Peptides
CJC-1295 (Mod GRF 1-29) & Ipamorelin & GHRP-2 Blend (9mg)
CJC-1295 (Mod GRF 1-29), Ipamorelin, and GHRP-2 are all synthetic peptides that are suggested by research teams to potentially stimulate the release of growth hormone. Anecdotal reports suggest that all three peptides appear synergistic when combined as a blend, potentially providing unique peptide action. CJC-1295 (Mod GRF 1-29) is considered to be an agonist to the receptors for the native Growth Hormone-Releasing Hormone (GHRH). It is an analog of its truncated version called GHRH (1-29) which appears to potentially have the same affinity to the receptors. GHRH 1-29 is potentially the shortest functional sequence of GHRH made up of its initial 29 amino acids. CJC-1295 (Mod GRF 1-29) is a variation that has undergone tetrasubstitution and has been further modified with the addition of a drug affinity complex (DAC) element named N-epsilon-3-maleimidopropionamide. This component may, perhaps, bind to plasma proteins, possibly enhancing the pharmacokinetics of CJC-1295 (Mod GRF 1-29). Ipamorelin is a pentapeptide that apparently mirrors the effects of the natural hunger hormone, ghrelin. This hormone may activate the ghrelin receptors in the pituitary gland, also known as the Growth Hormone Secretagogue receptors (GHS-R1a) which may trigger the release of growth hormone. GHRP-2, also known as Growth Hormone Releasing Peptide 2, is a hexapeptide crafted from six distinct amino acids. It is a synthetic peptide analogous to the receptors of the naturally occurring peptide called ghrelin (aka the GHS-R1a receptors). Thus, GHRP-2 and Ipamorelin peptides appear to trigger GHS-R1a and potentially stimulate the release of growth hormone. However, they may also possibly increase food intake due to their reported effect on ghrelin receptors. This is why they are classified by researchers as Growth Hormone Secretagogues (GHSs). Chemical Makeup (3)(4)(5) Molecular formula: CJC-1295 (Mod GRF 1-29): C152H252N44O42 Ipamorelin: C38H49N9O5 GHRP-2: C45H55N9O6 Molecular weight: CJC-1295 (Mod GRF 1-29): 3367.9 g/mol Ipamorelin: 711.9 g/mol GHRP-2: 817.9 g/mol Other known titles: Ipamorelin Ipamorelin Acetate, IPA GHRP-2 Pralmorelin, Growth hormone-releasing peptide-2 Research and Clinical Studies CJC-1295 (Mod GRF 1-29), Ipamorelin, GHRP-2 Blend and Growth Hormone Deficiencies Numerous clinical studies have been conducted on test subjects exhibiting growth hormone deficiency. These studies are recorded here for educational and research purposes; studies like these are ongoing and do not offer conclusive evidence of the peptide’s potential mechanism of action. In these clinical trials, peptides stimulating growth hormone release appeared to deliver some action in two ways – possibly either via stimulating the pituitary gland to release growth hormones, or possibly acting on the arcuate nucleus of the hypothalamus. While these peptides (including GHRP-2, Ipamorelin, and CJC-1295 (Mod GRF 1-29)) appeared to exhibit high releases of growth hormones, it remains unclear which of the two mechanisms worked. In addition, these studies suggested that these peptides may modulate food intake, cardiac tone, and sleep through apparently specific receptor agonistic action.(4) In another study,(5) six growth hormone-deficient test subjects facing growth failure were presented with growth hormone-stimulating peptides. All subjects were monitored for episodic growth hormone secretion and toxicity levels during this period. For the duration of the study and short while afterwards, It was observed that there appeared to be a gradual rise in the concentration of growth hormones in all subjects. As per V Mericq et al., the studies suggested that the peptides were “well tolerated and […] stimulate GH secretion.” Studies such as this one are still underway, and these peptides require further research. CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29), Ipamorelin, GHRP-2 Blend, and Food Intake In this clinical study,(6) test subjects were presented with GHRP-2 and then presented with unlimited food supply to measure food intake. It was reported that the subjects with peptide presence ate approximately 36% more than the control subjects did. In addition, the growth hormone levels were reportedly increased in these subjects, suggesting the action the peptides had on both food intake and growth hormone levels. As per this study, the growth hormone release-stimulating peptides appeared to be a “valuable tool for investigating the effects on eating behavior.” Research studies are still ongoing to fully explore the potential of peptide blends. Given its potential influence on the ghrelin receptors, Ipamoreline might also potentially enhance appetite and, perhaps, lead to weight gain. One study suggests that Ipamorelin may have possibly contributed to a roughly 15% rise in the body weight of the experimental subjects.(7) Researchers have posited the theory that Ipamorelin might have, to some extent, augmented the fat pad weights in proportion to overall body weight. This may have resulted in a relative increase in body fat as measured by dual energy X-ray absorptiometry (DEXA). Moreover, there is an indication that Ipamorelin might have elevated serum leptin levels, a hormone that is thought to play a role in energy and appetite regulation. Consequently, scientists speculated that the Ipamorelin groups might have experienced an uptick in food consumption leading to an apparent weight gain. Thus, Ipamorelin and GHRP-2 appear may potentially have synergistic effects on increasing hunger levels. On the other hand, CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29) has not been suggested to affect appetite. CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29), Ipamorelin, GHRP-2 Blend, and Bone Mass By apparently increasing growth hormone synthesis, all three peptides may potentially upregulate bone mineral density. Yet, Ipamorelin appears to be the most researched of these three peptides for this focus. In a particular study, murine subjects were either exposed to Ipamorelin or a control agent.(8) The potential effects of Ipamorelin on bone mineral density were monitored in real-time using dual X-ray absorptiometry (DXA) at specific locations, including the femur and L6 vertebrae. After the research duration, the murine subjects' femurs underwent analysis with mid-diaphyseal peripheral quantitative computed tomography (pQCT) scans. The findings tentatively indicate that the peptide might have contributed to a potential weight gain and a potential uptick in the overall tibial and vertebral BMC (bone mineral content) as observed via DXA, in contrast to the control set. Yet, when accounting for the weight gain in the total BMC, there seemed to be no notable difference as per the researchers. There might have been a slight increase in the bone mineral density (BMD) of the tibial region, but the overall and vertebral BMDs appeared to stay stable. The pQCT data perhaps suggests that the rise in cortical BMC may be attributed to a growth in the cross-sectional bone area, even though the cortical volumetric BMD seemingly stayed the same. Both the femur and L6 vertebrae volumes might have experienced a growth, but the volumetric BMDs did not appear to shift. These observations hint at the theory that the increase in both cortical and total BMC may potentially stem from improved bone growth leading to expanded bone dimensions, with the volumetric BMD staying consistent. The researchers further suggest that GHRPs may also increase BMC/BMD. CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29), Ipamorelin, GHRP-2 Blend, and Muscle Mass The main focus on CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29) & Ipamorelin & GHRP-2 research has been on the peptides’ potential synergy in regards to increasing muscle mass. Studies on murine models with a GHRH gene deletion (referred to as GHRHKO), hinted that CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29) may potentially have favorable action on lean mass.(9) When influenced by CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29), GHRHKO models appeared to retain typical lean weight and length, unlike the control groups which reportedly struggled to reach standard weight and dimensions. Furthermore, both the comparative lean mass and the underlying fat mass in all groups linked with the peptide seemed to stay consistent with control measurements in normal murine models. This suggests that CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29) might favorably impact muscle and bone structures without necessarily promoting heightened fat accumulation. The researchers also observed a potential uptick in overall pituitary RNA and GH mRNA due to CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29), implying a potential surge in somatotroph cells - the cells in the pituitary gland thought to generate growth hormone. This speculated cell growth was additionally supported by visual evidence from immunohistochemistry. Ipamorelin has also been proposed to increase lean mass, as suggested by the positive nitrogen balance reported in some preliminary studies. In a particular study, researchers sought to explore the potential metabolic effects of Ipamorelin on certain liver markers related to alpha-amino-nitrogen transformation during what might be steroid-induced catabolism. The team attempted to gauge the liver's ability to produce urea-N (CUNS), which could be an indicative measure of nitrogen processing in the liver. They observed potential variations in messenger RNA (mRNA) levels linked with liver urea cycle enzymes, assessed the general nitrogen equilibrium, and speculated on the nitrogen composition of different organs. Researchers suggested that Ipamorelin might have led to an approximate 20% decrease in CUNS in contrast to the catabolic condition potentially brought about by steroids. Moreover, it could have perhaps diminished the activity of urea cycle enzymes, reestablished nitrogen equilibrium, and maybe adjusted or enhanced the nitrogen levels in organs. CJC-1295 (Mod GRF 1-29) (Mod GRF 1-29) & Ipamorelin & GHRP-2 Peptide Blend is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 91976842, CJC1295 Without DAC. https://pubchem.ncbi.nlm.nih.gov/compound/CJC1295-Without-DAC. National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 9831659, Ipamorelin. https://pubchem.ncbi.nlm.nih.gov/compound/Ipamorelin. National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 6918245, Pralmorelin. https://pubchem.ncbi.nlm.nih.gov/compound/Pralmorelin. Rogério G. Gondo et al, Growth Hormone-Releasing Peptide-2 Stimulates GH Secretion in GH-Deficient Patients with Mutated GH-Releasing Hormone Receptor, The Journal of Clinical Endocrinology & Metabolism, Volume 86, Issue 7, 1 July 2001, Pages 3279–3283, https://doi.org/10.1210/jcem.86.7.7694. Mericq V, Cassorla F, Salazar T, Avila A, Iñiguez G, Bowers CY, Merriam GR. Effects of eight months treatment with graded doses of a growth hormone (GH)-releasing peptide in GH-deficient children. J Clin Endocrinol Metab. 1998 Jul;83(7):2355-60. https://pubmed.ncbi.nlm.nih.gov/9661608/ Laferrère, Blandine et al. “Growth hormone releasing peptide-2 (GHRP-2), like ghrelin, increases food intake in healthy men.” The Journal of clinical endocrinology and metabolism vol. 90,2 (2005): 611-4. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2824650/ Lall, S., Tung, L. Y., Ohlsson, C., Jansson, J. O., & Dickson, S. L. (2001). Growth hormone (GH)-independent stimulation of adiposity by GH secretagogues. Biochemical and biophysical research communications, 280(1), 132–138. https://doi.org/10.1006/bbrc.2000.4065 Svensson, J., Lall, S., Dickson, S. L., Bengtsson, B. A., Rømer, J., Ahnfelt-Rønne, I., Ohlsson, C., & Jansson, J. O. (2000). The GH secretagogues ipamorelin and GH-releasing peptide-6 increase bone mineral content in adult female rats. The Journal of endocrinology, 165(3), 569–577. https://doi.org/10.1677/joe.0.1650569 Alba M, Fintini D, Sagazio A, Lawrence B, Castaigne JP, Frohman LA, Salvatori R. Once-daily administration of CJC-1295, a long-acting growth hormone-releasing hormone (GHRH) analog, normalizes growth in the GHRH knockout mouse. Am J Physiol Endocrinol Metab. 2006 Dec;291(6):E1290-4. doi: 10.1152/ajpendo.00201.2006. Epub 2006 Jul 5. PMID: 16822960. Aagaard, N. K., Grøfte, T., Greisen, J., Malmlöf, K., Johansen, P. B., Grønbaek, H., Ørskov, H., Tygstrup, N., & Vilstrup, H. (2009). Growth hormone and growth hormone secretagogue effects on nitrogen balance and urea synthesis in steroid treated rats. Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society, 19(5), 426–431. https://doi.org/10.1016/j.ghir.2009.01.001 Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
Pancragen (20mg)
Pancragen is a tetrapeptide with the sequence Lys-Glu-Asp-Trp (KEDW). It is a synthetic structural analog of a peptide isolated from cattle pancreatic cells, which is posited to be a prospective peptide bioregulator for pancreatic function and aging-related metabolic problems. Pancragen has been suggested by researchers to act by penetrating cellular membranes and interacting with the nucleus and nucleolus. This suggests it could influence gene transcription associated with cell differentiation within the pancreatic cells. Key differentiation factors like Ptf1a, Pdx1, Pax6, Foxa2, Nkx2.2, and Pax4 are thought to play essential roles in the proper differentiation of pancreatic cells. Pancragen might up-regulate the expression of these factors, implying a positive action on the maturation of pancreatic cells. Pancragen may also influence the expression of molecules such as MMP2, MMP9, serotonin, CD79alpha, Mcl1, PCNA, and Ki67, suggesting it might boost the functional activity of pancreatic cells. Another mechanism may include a decrease in proapoptotic protein p53 and increase in antiapoptotic protein Mcl1 hinting at an antiapoptotic potential. Last but not least, Pancragen may influence aging biomarkers, reducing caspase-3 and cathepsin B activities and modulating levels of TNF-α and IGF-I. IGF-I, researched for its antiapoptotic actions, suggests that Pancragen's actions might be linked to metabolic correction and antiapoptotic mechanisms. Pancragen also seems to affect the methylation patterns of genes like PDX1, PAX6, and NGN3, which might mediate some of its anti-aging potential on the pancreatic cells. Chemical Makeup Molecular formula: C26H36N6O9 Molecular weight: 576.25 g/mol Sequence: Lys-Glu-Asp-Trp Other known titles: KEDW, DWa (amidate) Research and Clinical Studies In the information below, we have broken down the latest clinical and preclinical research on Pancragen’s potential as observed in various experimental models. Pancragen and the Pancreas The tetrapeptide Pancragen has been studied for its potential impact on pancreatic cells, particularly in relation to cell differentiation and the regulation of insulin and glucagon release, crucial elements in the pancreatic cells’ endocrine function. (1) Research posited that Pancragen might penetrate cellular membranes to interact with the nucleus and nucleolus, thereby possibly influencing the transcription of genes crucial for cellular differentiation within the pancreatic gland. Key differentiation factors such as Ptf1a, Pdx1, Pax6, Foxa2, Nkx2.2, and Pax4 are crucial for the proper functioning and differentiation of various pancreatic cell types. It is posited that Pancragen's interaction may potentially up-regulate the expression of these factors, which may play a role in the cellular maturation process of both acinar and islet cells in the pancreatic gland. The experiments conducted on embryonic cultures of pancreatic acinar cells in this study suggested that Pancragen might significantly enhance the expression of Ptf1a and Pdx1 proteins, which are known to be crucial for the maturation of acinar and islet cells. The study suggested that Pancragen's actions might be more pronounced in aged cultures, where an apparent decrease in the expression of these proteins is observed as a part of the cellular aging process. This potential up-regulation of key differentiation factors by Pancragen is posited to possibly lead to an increased differentiation of pancreatic cells, and, subsequently, may aid in restoring the functional activity of the pancreatic cells to a state akin to that observed in younger cell cultures. The researchers also posited that “transcription factors that regulate differentiation of pancreatic cells are a pharmacological target for Pancragen, which allows considering it as an effective tool in the treatment of diabetes mellitus and pancreatitis.” Another research study using murine models to gauge the impact of Pancragen on the pancreas's functional morphology, also yielded interesting findings.(2) Initially, when DM was induced in murine models, there was a noted decrease in insulin-producing B cells and an uptick in glucagon-producing A cells. Such changes point to disrupted pancreatic cell functionality. However, upon exposure to Pancragen, potentially encouraging shifts were observed. Murine models showed evident compensatory changes in pancreatic cells and tissue. Specifically, Pancragen seemed to bolster insulin production from B cells while tempering glucagon production from A cells. Additionally, the proliferative activity of certain cells and their apoptosis seemed to normalize, closely resembling control murine models. Further research has also suggested that Pancragen might play a pivotal role in the modulation of various cellular markers and proteins associated with the vitality of pancreatic cells. When applied to aging pancreatic cells, there was an observed increase in the expression of matrix metalloproteinase MMP2 and MMP9, serotonin, glycoprotein CD79alpha, the antiapoptotic protein Mcl1, and proliferation markers PCNA and Ki67. Conversely, there was a decrease in the expression of the proapoptotic protein p53 in aged pancreatic cell cultures. From these observations, it can be posited that the tetrapeptide potentially holds the capability to activate the expression of signaling molecules that serve as markers of the functional activity of pancreatic cells.(3) Pancragen and Metabolic Problems Studies have delved into the potential of Pancragen on metabolic problems in aged test subjects. For example, in one study, the focus was mainly on carbohydrate metabolism and the potential role Pancragen may play in regulating it.(4) The introduction of Pancragen was observed to significantly lower fasting glucose levels during a standard glucose tolerance test, alongside a reduction in insulin concentrations and the insulin resistance index. This suggests a potential utility of Pancragen in addressing the disturbances in carbohydrate metabolism, especially given the observed persistence of its glucose-lowering action post-exposure. It is critical to note that the study was focused on august test subjects, and the scope of Pancragen’s potential may be contingent on several other variables, including the severity of insulin resistance and other factors. The researchers also commented that “Administration of the tetrapeptide Pancragen is a promising approach to the correction of insulin resistance in elderly.” Another study aimed to investigate the potential impact of Pancragen on the endocrine function of the pancreatic cells and the metabolic status of test models.(5) Aged test models used in this research were used to understand the potential of Pancragen in addressing age-related dysfunctions in the overall metabolism as well as the pancreatic islet apparatus. In older test models, there was a noted reduced rate of glucose utilization compared to younger counterparts. Moreover, higher insulin and C-peptide peaks were observed 5 and 15 minutes post-glucose introduction. However, when Pancragen was introduced per test model daily over 10 days, there was a marked improvement in the glucose utilization rate. This intervention also seemed to normalize the dynamics of plasma insulin and C-peptide in response to glucose. Intriguingly, the actions of Pancragen lingered, with some aspects of metabolic status and pancreatic cell function remaining improved even three weeks after the cessation of the trial. In a study examining the actions of Pancragen on endothelial function within the setting of chronic hyperglycemia using murine models, it was observed that the introduction of Pancragen may have potential role in restoring endothelial adhesive characteristics. (6) Restoring these endothelial adhesive characteristics is crucial because, in models of metabolic problems, proper endothelial function plays a vital role in blood flow regulation and preventing complications such as atherosclerosis. Deficiencies or abnormalities in endothelial adhesion may increase susceptibility to vascular damage, making this restoration a key target for averting it. Pancragen and Aging Pancragen has been posited as a possible bioregulator for adjusting metabolic problems associated with aging. To understand Pancragen's impact on aging, a study examined its potential on murine models across different age groups.(7) There was a noted decrease in certain aging biomarkers like caspase-3 and cathepsin B activities when Pancragen was introduced to the younger murine models. Interestingly, in the mature murine models, Pancragen application resulted in a significant reduction of TNF-α levels and an elevation in IGF-I, both of which are critical indicators related to aging and metabolic processes. The study also delved into a rapid experimental aging model by inducing diabetes mellitus in murine models. It was observed that Pancragen potentially normalized blood glucose levels, emphasizing its previously identified hypoglycemic properties. Furthermore, the presence of Pancragen might have suppressed certain apoptotic enzymatic components in the pancreatic cells, suggesting that its biological actions may be associated with both metabolic correction and antiapoptotic mechanisms. The actions of Pancragen on natural biological aging are potentially realized at the IGF-I level, known for its "survival factor" antiapoptotic actions. Moreover, the tetrapeptide's potential interaction with certain genes suggests that its influence might extend to the proteolytic processing level. According to another trial, Pancragen has been posited to tissue-specifically influence gene expression in pancreatic cell cultures.(8) The study suggests that variations in the methylation patterns of the PDX1, PAX6, and NGN3 gene promoter regions in pancreatic cells may be associated with aging and could potentially be the cause behind the alterations in their expression levels. This implies that long-standing changes in gene expression upon aging might be driven by modifications in these promoter methylation patterns. However, the expression levels of the PAX4 and FOXA2 genes in pancreatic cells seem to deviate during aging and in response to Pancragen, even when the methylation patterns of the PAX4 gene remain stable. Curiously, the FOXA2 gene's promoter region in pancreatic cells exhibited only a handful of methylated CpG sites, with their methylation levels being influenced by both cell culture aging and Pancragen. Yet, this did not correlate straightforwardly with changes in gene expression levels. This suggests that, despite the influence of Pancragen on certain gene methylation patterns, the exact relationship between methylation and gene expression may be intricate and possibly regulated by other, yet unidentified, mechanisms. Pancragen peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Khavinson, V. K.h, Durnova, A. O., Polyakova, V. O., Tolibova, G. H., Linkova, N. S., Kvetnoy, I. M., Kvetnaia, T. V., & Tarnovskaya, S. I. (2013). Effects of pancragen on the differentiation of pancreatic cells during their ageing. Bulletin of experimental biology and medicine, 154(4), 501–504. https://doi.org/10.1007/s10517-013-1987-6 Kvetnoi, I. M., Ryzhak, A. P., Kostyuchek, I. N., & Tafeev, Y. A. (2007). Effect of tetrapeptide pancragene on functional morphology of the pancreas in rats with experimental diabetes mellitus. Bulletin of experimental biology and medicine, 143(3), 368–371. https://doi.org/10.1007/s10517-007-0114-y Khavinson, V. K.h, Sevost'ianova, N. N., Durnova, A. O., Lin'kova, N. S., Tarnovskaia, S. I., Dudkov, A. V., & Kvetnaia, T. V. (2012). Advances in gerontology = Uspekhi gerontologii, 25(4), 680–684. Korkushko, O. V., Khavinson, V. K.h, Shatilo, V. B., Antonyk-Sheglova, I. A., & Bondarenko, E. V. (2011). Prospects of using pancragen for correction of metabolic disorders in elderly people. Bulletin of experimental biology and medicine, 151(4), 454–456. https://doi.org/10.1007/s10517-011-1354-4 Goncharova, N. D., Ivanova, L. G., Oganyan, T. E., Vengerin, A. A., & Khavinson, V. K. (2015). Advances in gerontology = Uspekhi gerontologii, 28(3), 579–585. Khavinson, V. K.h, Gavrisheva, N. A., Malinin, V. V., Chefu, S. G., & Trofimov, E. L. (2007). Effect of pancragen on blood glucose level, capillary permeability and adhesion in rats with experimental diabetes mellitus. Bulletin of experimental biology and medicine, 144(4), 559–562. https://doi.org/10.1007/s10517-007-0377-3 Khavinson, V. K.h, Gapparov, M. M., Sharanova, N. E., Vasilyev, A. V., & Ryzhak, G. A. (2010). Study of biological activity of Lys-Glu-Asp-Trp-NH2 endogenous tetrapeptide. Bulletin of experimental biology and medicine, 149(3), 351–353. https://doi.org/10.1007/s10517-010-0944-x Ashapkin, V. V., Linkova, N. S., Khavinson, V. K.h, & Vanyushin, B. F. (2015). Epigenetic mechanisms of peptidergic regulation of gene expression during aging of human cells. Biochemistry. Biokhimiia, 80(3), 310–322. https://doi.org/10.1134/S0006297915030062 Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
Vesugen (20mg)
Vesugen, aka KED, is a bioregulator peptide and identified within the group of peptides isolated and synthesized by Russian scientist, Vladimir Khavinson. It is a tripeptide derived from a sequence of amino acids related to vascular wall proteins, encapsulating the amino acids lysine, glutamic acid, and aspartic acid. Vesugen is primarily known for its potential influence on vascular endothelial cells. Further, its potential extends to a wide array of biological processes, making it a viable research compound within the context of anti-aging and neuroprotection research. Primarily, Vesugen is recognized for its potential vasoprotective impacts, with a particular emphasis on its role in the maintenance and repair of vascular endothelial cells. These cells form the lining of blood vessels. In addition to its vascular implications, Vesugen has also been explored for its neuroprotective and geroprotective consequences. Studies have examined its effects on neuron survival and morphology, suggesting its possible role in combating neurodegenerative diseases and enhancing neuroplasticity. Chemical Makeup Molecular formula: C15H26N4O8 Molecular weight: 390.39 g/mol Sequence: Lys-Glu-Asp Other known titles: KED, lysyl glutamyl aspartic acid, SCHEMBL3767701 Vesugen Research and Clinical Studies The information provided below synthesizes the latest insights from early-stage research regarding the capabilities of Vesugen, as demonstrated through a variety of experimental approaches. Vesugen and Vasoprotective Potential Vasugen may have vasoprotective potential, particularly relevant in the context of aging and vascular function. This potential is primarily attributed to its proposed ability to influence the behavior of vascular endothelial cells. The available research posits that Vesugen may exert vasoprotective action through the modulation of cell proliferation.(1) It is thought to do this by potentially regulating the expression of the Ki-67 protein, a marker that is closely associated with cellular proliferation. This protein's expression seemingly decreases as part of the natural aging process, affecting the vascular endothelium's ability to renew itself. Vesugen is hypothesized to interact with the promoter regions of the Ki-67 gene, potentially leading to increased expression of this protein. The possible impact of Vesugen on vascular endothelial cells includes the stimulation of cell proliferation. By potentially enhancing the expression of Ki-67, Vesugen might contribute to the maintenance or restoration of the integrity and function of the vascular endothelium. This may be particularly relevant in addressing age-related vascular function problems, including issues such as reduced proliferative capacity and the increasing prevalence of polyploid cells, which may contribute to vascular lesions and atherosclerosis. Moreover, the study suggests that Vesugen might interact with DNA at specific sites, influencing gene expression in a way that may favor vascular function. This interaction is thought to occur mainly in the minor groove of DNA, with Vesugen forming hydrogen bonds with specific DNA base pairs. Ultimately, the researchers concluded that the “vasoprotective effect of peptide vesugen ... could be realized through epigenetic regulation of Ki-67 gene expression.” The presumed mechanism underlying its potential effects of Vesugen may involve the epigenetic regulation of genes thought to code for proteins that serve as markers of endothelial functional activity, crucial in cardiovascular function. In vitro investigations into Vesugen's impact on endothelial cells, particularly those impacted by atherosclerosis and restenosis, suggest that it may help normalize the expression of endothelin-1.(2) This molecule's expression typically rises in atherosclerotic and restenotic conditions, suggesting that Vesugen could possibly play a role in addressing these pathologies. Moreover, Vesugen appears to potentially aid in restoring cellular interactions, possibly through its influence on connexin expression. Connexins are vital for cell-to-cell communication, which is essential for maintaining endothelial integrity and function. An additional aspect of Vesugen's potential action is its apparent geroprotective effect, potentially achieved by increasing the expression of sirtuin1, a protein involved in DNA repair. This increase in sirtuin1 expression might be significant for cardiovascular function, as it may contribute to the mitigation of damage at the genetic level. Vesugen and Neuroprotective Potential Investigation into Vesugen’s neuroprotective potential within the context of neurodegeneration has elaborated on the apparent impact of the peptide on neuroplasticity and neuron morphology in murine models simulating certain neurodegeneration conditions.(3) A key aspect of this research was the examination of long-term potentiation (LTP) in the hippocampus, a crucial area for memory and learning. The neurodegenerated murine models showed a trend toward impaired neuroplasticity compared to wild-type murine models, particularly after high-frequency stimulation of Schaffer’s collaterals. However, this observed impairment in neuroplasticity was not statistically significant, suggesting only a subtle action. The exposure to the Vesugen peptide in these murine models suggested a potential to restore LTP, suggesting a role in enhancing neuroplasticity. Despite this positive suggestion, the action of the Vesugen peptide on restoring LTP also did not reach statistical significance, leaving its impact as a promising yet unconfirmed hypothesis. Furthermore, the study delved into the action of Vesugen peptide on neuron morphology, specifically focusing on the dendritic spine density in the CA1 region of the hippocampus. This area is vital for synaptic connections and is notably affected in neurodegeneration. The research found that the introduction of the Vesugen peptide helped prevent the elimination of postsynaptic structures in CA1 neurons of the neurodegeneration murine models. Interestingly, the most pronounced action of Vesugen was observed in the restoration of mushroom and thin spines, which are critical for synaptic strength and memory. This finding aligns with literature data on spine balancing in neurodegeneration progression, suggesting a modulatory action of Vesugen on spine morphology. Moreover, the study noted sex-related differences in the neuroprotective action of Vesugen peptide in neurodegeneration murine models. In male models, Vesugen peptide significantly increased dendritic spine density and restored mushroom spine numbers, suggesting a gender-specific response in neuroprotective action. The authors commented that the neuroprotective potential of Vesugen and similar peptides is “defined by their ability to prevent dendritic spine elimination and neuroplasticity impairments at the molecular epigenetic level.” Another trial aimed to investigate the mechanisms behind the potential of Vesugen in addressing neurodegenerative conditions.(4) The primary focus was on its influence on gene expression and protein synthesis, which are crucial in processes like apoptosis, aging, neurogenesis, and, more specifically, neurodegeneration. Experimental findings, coupled with published reports, suggest that Vesugen may play a role in regulating the expression of genes associated with cell aging and apoptosis, such as р16 and р21. These genes are pivotal in determining the lifespan of cells and their programmed death, which are critical factors in neurodegenerative diseases. Moreover, Vesugen appears to affect genes and proteins that are involved in neuronal differentiation, such as NES (Nestin) and GAP43. Nestin is a type of intermediate filament protein potentially involved in the structural support of cells, particularly in the early stages of development in the nervous system. GAP43, on the other hand, is a protein that may play a key role in axonal growth during neural development and in the regeneration of neurons. The modulation of these genes and proteins by Vesugen might be integral in fostering neurogenesis, a process that may be beneficial in countering neurodegenerative processes. Furthermore, the peptide seems to interact with genes implicated in the pathogenesis of neurodegeneration. These include SUMO, APOE, and IGF1. SUMOylation, a post-translational modification involving the SUMO protein, is known to be involved in a variety of cellular processes, including transcriptional regulation, DNA repair, and protein stability – all of which are critical in the context of neurodegeneration. APOE, or apolipoprotein E, has been extensively studied for its role in lipid metabolism and its significant association with neurodegenerative diseases. Lastly, IGF1, or Insulin-like Growth Factor 1, is a hormone crucial for brain development and is thought to have neuroprotective properties. Vesugen and Geroprotective Potential Vesugen may potentially influence the behavior of prostatic fibroblasts, particularly concerning the expression of certain differentiation factors. This potential was observed in contexts where these cells exhibited signs of aging, suggested by reduced expression of differentiation markers in late-passage cultures.(5) Specifically, Vesugen is posited to stimulate the expression of CXCL12 and WEGC1 in these prostatic fibroblasts. CXCL12, also known as stromal cell-derived factor 1 (SDF-1), is a chemokine, a type of signaling protein. It is primarily indentified for its potential in the immune system, where it may aid in the regulation of immune cell movement. CXCL12 may also be involved in other biological processes, such as hematopoiesis (the formation of blood cellular components) and angiogenesis (the formation of new blood vessels). Its significance in cellular signaling may extend to influencing cell migration and activation, although the full scope of its actions and interactions in various tissues is still a subject of ongoing research. WEGC1, on the other hand, is less extensively studied, and its role is not as clearly defined in the literature. It might be involved in cellular differentiation processes, particularly in specific types of cells like fibroblasts. The exact functions of WEGC1, including how it influences cell behavior and interacts with other cellular components, are areas that require more detailed exploration. Its identification in studies concerning cellular aging and differentiation, such as those involving Vesugen, suggests that it could have a role in these processes, but the extent and nature of this role are yet to be fully elucidated. Most notably, the potential of Vesugen seemed to be more pronounced in aged cultures. This suggests, albeit with a degree of uncertainty, that Vesugen might exhibit geroprotective action, potentially supporting the maintenance or rejuvenation of cellular functions that decline with age. Clinical research has also aimed to explore Vesugen's potential in modifying biological age markers, a key aspect of aging, and thus its geroprotective potential.(6) Vesugen reportedly exhibited a notable anabolic effect, which is linked to improved activity in the central nervous system and other vital organs. This action was associated with a potential slowing of the aging process according to biological age indicators. An interesting aspect of the study was the observation of prooxidant activity through chemiluminescence. This suggests that Vesugen may induce some oxidative processes. Additionally, there was a reported decrease in CD34+ positive hematopoietic polypotent cells in the blood, suggesting a potential inhibition of hemopoiesis. This finding suggests these cells might not be actively involved in adaptive reactions during the appreciation of Vesugen. Vesugen peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Khavinson, V. K.h, Tarnovskaia, S. I., Lin'kova, N. S., Guton, E. O., & Elashkina, E. V. (2014). Advances in gerontology = Uspekhi gerontologii, 27(1), 108–114. Kozlov KL, Bolotov II, Linkova NS, Drobintseva AO, Khavinson VK, Dyakonov MM, Kozina LS. [Molecular aspects of vasoprotective peptide KED activity during atherosclerosis and restenosis]. Adv Gerontol. 2016;29(4):646-650. Russian. PMID: 28539025. Khavinson V, Ilina A, Kraskovskaya N, Linkova N, Kolchina N, Mironova E, Erofeev A, Petukhov M. Neuroprotective Effects of Tripeptides-Epigenetic Regulators in Mouse Model of Alzheimer's Disease. Pharmaceuticals (Basel). 2021 May 27;14(6):515. doi: 10.3390/ph14060515. PMID: 34071923; PMCID: PMC8227791. Khavinson VK, Lin'kova NS, Umnov RS. Peptide KED: Molecular-Genetic Aspects of Neurogenesis Regulation in Alzheimer's Disease. Bull Exp Biol Med. 2021 May;171(2):190-193. doi: 10.1007/s10517-021-05192-6. Epub 2021 Jun 26. PMID: 34173097. Khavinson VKh, Linkova NS, Polyakova VO, Kheifets OV, Tarnovskaya SI, Kvetnoy IM. Peptides tissue-specifically stimulate cell differentiation during their aging. Bull Exp Biol Med. 2012 May;153(1):148-51. doi: 10.1007/s10517-012-1664-1. PMID: 22808515. Meshchaninov VN, Tkachenko EL, Zharkov SV, Gavrilov IV, Katyreva IuE. [EFFECT OF SYNTHETIC PEPTIDES ON AGING OF PATIENTS WITH CHRONIC POLYMORBIDITY AND ORGANIC BRAIN SYNDROME OF THE CENTRAL NERVOUS SYSTEM IN REMISSION]. Adv Gerontol. 2015;28(1):62-7. Russian. PMID: 26390612. Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
Lipopeptide (200mg)
Lipopeptide, characterized by the sequence Palmitoyl-Gly-Gln-Pro-Arg, is a palmitoylated fragment derived from immunoglobulin G (IgG). IgG is a type of antibody, considered a crucial component of the immune system that apparently mediates various inflammatory processes. The palmitoylation of this peptide fragment, which involves the attachment of a palmitic acid molecule, may also enhance its experimental potential. This modification appears to improve the lipopeptide's ability to penetrate through the corneal layers of skin tissue models. The increased penetration appears to be due to the added lipid (fat) component, which aids in traversing the lipid-rich environment of the outer layers of skin tissue. Chemical Makeup Molecular formula: C38H68N6O8 Molecular weight: 736.9 g/mol Sequence: Pal-Gly-Gln-Pro-Arg Other known titles: Pal-GQPR, Palmitoyl Tetrapeptide-7/3 Research and Clinical Studies The summary below reflects the latest findings from preliminary studies on the functionalities of Lipopeptide, as revealed through diverse experimental methods. Lipopeptide and the Extracellular Dermal Matrix One study conducted a series of evaluations on a blend of peptides including Lipopeptide (Pal-GQPR) for their potential action on skin cell structure.(1) Echography tests suggested that this blend might reduce the thickness of the subepidermal low-echogenic band and support its density, indicating a possible improvement in skin structure. Moreover, studies in murine models hinted that these peptides might potentially enhance the extracellular dermal matrix structure compared to a placebo. More specifically it was posited that this compound might also play a role in decreasing the secretion of interleukin-6 (IL-6), a cytokine involved in inflammatory responses. IL-6 is a molecule that is typically associated with immune responses and appears to be elevated during inflammation, potentially contributing to various inflammatory skin conditions. The possible reduction of IL-6 secretion by Lipopeptide suggests that it may aid in mitigating inflammation, especially following UVB radiation exposure, a common cause of skin cell inflammation and damage. Additionally, Lipopeptide is thought to potentially stimulate the production of critical structural components around skin cells, such as laminin IV and V, as well as collagen VII. Laminins, particularly types IV and V, are integral components of the basement membrane, a layer that supports epithelial cells and is considered essential for tissue integrity. They play a crucial role in cell adhesion, differentiation, and migration, which are vital for skin repair and maintenance. Collagen VII, on the other hand, is a key component of anchoring fibrils that provide structural support and stability to the skin. It is essential for the attachment of the epidermis to the underlying dermis. The stimulation of these components by Lipopeptide may imply a potential role in enhancing the skin's structural framework.(2) Other researchers have also commented that Lipopeptide may have an action “as an anti-inflammatory agent and has anti-aging and skin firming [potential].”(3) Lipopeptide and Photoaged Skin Cells The potential of Lipopeptide was investigated in a randomized controlled trial (RCT) as a blend alongside other peptides and active ingredients. This peptide, along with other compounds, such as retinyl palmitate and natural extracts, was assessed for its potential in improving the appearance of photoaged skin cells. Twelve days into the experiment, the peptide was observed to have stimulated the deposition of fibrillin-1 in the skin, a marker for skin repair, compared to the baseline levels. This was comparable to the apparent results observed with all-trans retinoic acid (RA), considered to be a clinical standard for photoaged skin cells. The accumulation of fibrillin-1 indicates a potential structural change in the skin, although this alone does not confirm the success of the experiment. In a 6-month RCT the peptide appeared to potentiate an improvement in skin wrinkles compared to the baseline. Interestingly, this potential improvement became more pronounced after 12 months. The vehicle formulation, which lacked the active ingredients, did not show similar results, suggesting that the ingredients in the test product, including Lipopeptide, may contribute to the observed effects. Furthermore, the study investigated the distribution of fibrillin-1 in skin biopsies from the RCT. Skin applied with the Lipopeptide appeared to have a significant increase in fibrillin-1 in the papillary dermis compared to the placebo group. This supports the idea that long-term experiments with Lipopeptide may lead to a visible improvement in the photoaged skin. The researchers concluded that Lipopeptide may “produce significant improvement in the appearance of wrinkles and further supports the [study] of fibrillin-1 as a robust biomarker for the repair of photoaged dermis.”(4) Lipopeptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Mondon, P., Hillion, M., Peschard, O., Andre, N., Marchand, T., Doridot, E., Feuilloley, M. G., Pionneau, C., & Chardonnet, S. (2015). Evaluation of dermal extracellular matrix and epidermal-dermal junction modifications using matrix-assisted laser desorption/ionization mass spectrometric imaging, in vivo reflectance confocal microscopy, echography, and histology: effect of age and peptide applications. Journal of cosmetic dermatology, 14(2), 152–160. https://doi.org/10.1111/jocd.12135 Resende, D. I. S. P., Ferreira, M. S., Sousa-Lobo, J. M., Sousa, E., & Almeida, I. F. (2021). Usage of Synthetic Peptides in Cosmetics for Sensitive Skin. Pharmaceuticals (Basel, Switzerland), 14(8), 702. https://doi.org/10.3390/ph14080702 Fadilah, N. I. M., Rahman, M. B. A., Yusof, L. M., Mustapha, N. M., & Ahmad, H. (2021). The Therapeutic Effect and In Vivo Assessment of Palmitoyl-GDPH on the Wound Healing Process. Pharmaceutics, 13(2), 193. https://doi.org/10.3390/pharmaceutics13020193 Watson, R. E., Ogden, S., Cotterell, L. F., Bowden, J. J., Bastrilles, J. Y., Long, S. P., & Griffiths, C. E. (2009). Effects of a cosmetic 'anti-ageing' product improves photoaged skin [corrected]. The British journal of dermatology, 161(2), 419–426. https://doi.org/10.1111/j.1365-2133.2009.09216.x Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
PEG-MGF (5mg)
MGF is an acronym for Mechano Growth Factor, a research peptide that scientists consider to belong to the class of IGF-1 (insulin-like growth factor) family.(1) An isoform of IGF-1, MGF is also known as IGF-1Ec, and is believed to primarily be produced in the liver.(2) The IGF-1 gene appears to undergo transcription and may generate the three mRNA isoforms: IGF-1Ea, IGF-1Eb, and IGF-1Ec. This indicates that MGF (or IGF-1Ec) may be identical to IGF-1 but with a different E domain. Synthesis of each isoform appears to possess specific functions in different tissues as a response to diverse stimuli. PEG-MGF, or polyethylene glycol (PEG)-ylated MGF, is a synthetic form of MGF. Pegylation connects polyethylene glycol (PEG) to another compound to alter its structure. Scientists consider that MGF by itself may have a short half-life; however, once bound with PEG, the half-life may be extended by some days. Research studies posit that PEG IGF-1 may be more impactful than recombinant IGF-1 for muscle cell regeneration and improving muscle function. The main reasoning was attributed to the hypothesis that PEG may not easily bind with any other compounds, and may thereby lead to delayed clearance. In addition, modifying the C terminus of IGF-1 with the addition of PEG may increase the peptide's potential impact on tissues.(3) Overview Researchers suggested the existence of three IGF-1 precursor proteins formed upon the splicing of the mature IGF-1. Each precursor comprises 70 amino acid residues from the mature IGF-1, and may only differ in the amino acid sequence attached to the COOH terminal, possibly determining its function. During the late 1990s and early 2000s, it was suggested that one of the three precursors, IGF-1EC (MGF), may increase upon muscle injury.(4) Several studies have been carried out thereafter(3) to isolate and synthesize the (PEG)-ylated MGF to modify and potentially improve the impact and action of the peptide. The studies have suggested that under muscle stress the mature IGF-1 may become spliced as a response to stress and may thereby produce and release one of the isoforms called IGF-1EC, also known as Mechano Growth Factor (MGF).(4) One research hypothesis suggests that as MGF increases, the amino acid sequence attached to the COOH terminal of MGF may become activated and promote cell proliferation in muscle stem cells. Further studies indicated that PEG-MGF may stimulate the proliferation of C2C12 muscle cells and myoblasts upon presentation. Based on these results, it was suggested that the MGF peptide may be biologically active and inert by nature. PEG-MGF may induce stronger, more durable action of normal MGF. Chemical Makeup Molecular Formula: C121H200N42O39 Molecular Weight: N/A Other Known Titles: PEG-MGF-E, PEG-MGF-Ct24E Research and Clinical Studies PEG-MGF Peptide and Muscle Structure Muscle resistance activity seems to activate mechano-growth factor (MGF) mRNA in muscle tissues, which researchers suggest manifests as a substantial 163% rise from baseline levels.(5) This pronounced increase suggests a potentially direct response of MGF to mechanical stimuli within the muscles. Concurrently, an observed surge in growth hormone levels, which typically accompanies muscle resistance, may add complexity to this molecular interplay. Data suggests a 456% augmentation in MGF mRNA coinciding with resistance activities, whereas an increase in growth hormone levels alone appears to influence MGF mRNA expression by about 80% compared to baseline. The scientists commented “This may reflect an overall up-regulation of transcription of the IGF-I gene prior to splicing.” Consequently, it is hypothesized that MGF may play a critical role in the organism’s intrinsic mechanism to mitigate muscle damage and promote tissue repair in response to mechanical stress. This hypothesis underscores the intricate and coordinated molecular responses triggered by physical exertion, reflecting a sophisticated biological adaptation to preserve muscle integrity and function. To further investigate this, a study(6) was conducted to examine the potential of MGF on muscle repair and wound healing. Experimental murine models induced with muscle contusion and muscular macrophage depletion were used as study subjects. Based on comprehensive analyses following the study, the researchers theorized that MGF might induce muscular repair in the wounded tissues. MGF appeared to decline the rate of fibrosis in the contused muscles and reduced the expressions of inflammatory cytokines, chemokines, and stress factors. Preliminary analyses indicated that MGF might affect fibrosis in damaged muscle tissue through the likely suppression of collagen types I and III expression. These collagens are considered essential components of the extracellular matrix involved in fibrotic processes. Additionally, there appeared to be a noticeable decrease in oxidative stress markers and matrix metalloproteinases (MMPs), which might suggest that MGF may attenuate certain inflammatory processes associated with muscle injury. Moreover, the prevalence of contused muscles seemed to decrease, potentially facilitating the repair mechanisms in the injured tissues. The investigation also proposed that MGF's influence on the functional dynamics of satellite cells post-injury and immune cell presence at the injury site—both deemed critical to muscle regeneration—might be minimal. This proposition is based on the stable expression levels of MyoD and myogenin, which are considered to be pivotal markers of satellite cell proliferation and differentiation, respectively. Therefore, while MGF may alleviate some facets of the muscle injury response, its direct impact on satellite cell functionality in these specific circumstances may not definitively be established. The study further suggested that MGF might modify the inflammatory environment within the injured muscle tissue. This modulation is tentatively evidenced by a reported decrease in the expression of pro-inflammatory cytokines such as tumor necrosis factor-alpha (TNF-α), interferon-gamma (IFN-γ), interleukin-1 beta (IL-1β), and transforming growth factor-beta (TGF-β), alongside chemokines like CCL2, CCL5, and CXCR4 following MGF experimentation. Additionally, there was a speculative indication that MGF might help mitigate oxidative stress in injured muscles, as suggested by a possible reduction in the expression of gp91phox, an element of NADPH oxidase that appears to play a significant role in the generation of reactive oxygen species. PEG-MGF Peptide and Cardioprotection The main goal of this study(7) was to evaluate the potential of MGF action on cardiac muscles undergoing programmed cell death following hypoxia, a condition characterized by limited supply of oxygen. Rats were experimentally induced with hypoxia with only 1% oxygen supply, leading to cellular apoptosis. Once the peptide was given to the rat models, the study reported that the peptide appeared to induce increased migration of stem cells to the heart, possibly leading to apoptosis inhibition. More specifically, MGF is suggested to potentially enhance the migration of mesenchymal stem cells (hMSCs). This process suggests a chemotactic action, which may be strategically employed to guide stem cells to areas affected by injury or disease. The basis for this proposition stems from apparent increases in the levels of the Bcl-2 gene, which is believed to play a critical role in enhancing cell survival, thus suggesting that MGF may possess qualities that inhibit apoptotic processes in cells. This observation underscores the possibility of MGF as a potential agent in enhancing tissue regeneration by modulating cellular mechanisms that may prevent programmed cell death. PEG-MGF Peptide and Bone Fracture The main goal of this study(8) was to evaluate the potential of MGF on bone injury. 27 rabbits were experimentally induced with a 5-mm bone defect and were then divided into three groups that were given MGF, or a control substance for 5 consecutive days. Post-trial, when the bone tissues were histologically examined, the researchers reported that the control tissue appeared to be the least healed, whereas the bone tissue with MGF appeared to be the most healed. Comparatively, MGF-exposed tissues also exhibited a superior healing process relative to those exposed to Insulin-like Growth Factor 1 (IGF-1), suggesting that MGF may interact with cellular processes in a distinct manner from IGF-1. Further insights from the study suggest that MGF might influence the cell cycle by potentially halting it at specific stages, and it may also activate the Mitogen-Activated Protein Kinase/Extracellular Signal-Regulated Kinase 1/2 (MAPK-Erk1/2) signaling pathway. These mechanisms indicate that MGF might employ a multifaceted strategy to enhance cell proliferation, which likely involves altering cell cycle progression and triggering particular molecular pathways crucial for cellular repair and regeneration. This nuanced approach underscores MGF's potentially complex and targeted action in bone healing models. PEG-MGF Peptide and Neuroprotection Several studies(9) were conducted on mice who were experimented on in order to increase the levels of MGF and thereby study the action of increased MGF concentration on their brain cells. One study included the breeding of mice to constitutively overproduce MGF in the hippocampus area of the brain. The hippocampus is considered primarily responsible for regulating the neurogenesis phenomenon in the body. This overproduction of MGF appeared to result in high concentrations of BrdU, a biological marker representative of proliferative action. Another study was conducted where mice were bred to conditional MGF production at 1, 3, and 12 months old. Behavioral analysis and biological responses were examined after 2 years. These mice were reported to exhibit elevated levels of BrdU and neurogenesis. MGF Peptide and Muscle Tissue Hypertrophy The main aim of one pivotal study on MGF(10) was to assess its potential on muscle cells of varying ages. In this study, muscle cell cultures, from neonatal to aged stages, underwent evaluation after being exposed to MGF. It was observed that in younger cells, MGF seemed to postpone the onset of cellular senescence, which is the gradual deterioration of cellular function. This delay suggests that MGF might be able to maintain muscle function and its regenerative properties, which typically decline with age. Additionally, the study noted an enhancement in cell proliferation among cells ranging from neonatal to young; however, such proliferation did not appear to extend to the older aged cells. In these older cells, there was a noticeable increase in muscle hypertrophy, characterized by an augmented muscle cell size. Yet, there was a marked reduction in the number of reserve cells. These reserve cells, which typically do not immediately differentiate or amalgamate into myotubes, were apparently at a reduced proportion in the culture. Myotubes, crucial structures in muscle development, are formed through the fusion of muscle cells. This fusion process was apparently enhanced across all age groups by MGF, which not only increased the myotube size but potentially also the muscle’s functional capabilities through the augmented expression of muscle-specific contractile proteins. This observation is significant as it implicates a reduced presence of reserve cells, suggesting that MGF might encourage these cells to participate more actively in muscle formation. In conclusion, the researchers posited that “MGF-24aa-E peptide alone has a marked ability to enhance satellite cell activation, proliferation and fusion for muscle repair and maintenance.” PEG-MGF is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Philippou A, Papageorgiou E, Bogdanis G, Halapas A, Sourla A, Maridaki M, Pissimissis N, Koutsilieris M. Expression of IGF-1 isoforms after exercise-induced muscle damage in humans: characterization of the MGF E peptide actions in vitro. In Vivo. 2009 Jul-Aug;23(4):567-75. https://pubmed.ncbi.nlm.nih.gov/19567392/ Zabłocka, B., Goldspink, P. H., Goldspink, G., & Górecki, D. C. (2012). Mechano-Growth Factor: an important cog or a loose screw in the repair machinery? Frontiers in endocrinology, 3, 131. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3485521/ Janssen, J. A., Hofland, L. J., Strasburger, C. J., van den Dungen, E. S., & Thevis, M. (2016). Potency of Full-Length MGF to Induce Maximal Activation of the IGF-I R Is Similar to Recombinant Human IGF-I at High Equimolar Concentrations. PloS one, 11(3), e0150453. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4798685/ Rotwein P. (2014). Editorial: the fall of mechanogrowth factor?. Molecular endocrinology (Baltimore, Md.), 28(2), 155–156. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3896639/ Hameed M, Lange KH, Andersen JL, Schjerling P, Kjaer M, Harridge SD, Goldspink G. The effect of recombinant human growth hormone and resistance training on IGF-I mRNA expression in the muscles of elderly men. J Physiol. 2004 Feb 15;555(Pt 1):231-40. doi: 10.1113/jphysiol.2003.051722. Epub 2003 Oct 17. PMID: 14565994; PMCID: PMC1664832. Liu X, Zeng Z, Zhao L, Chen P, Xiao W. Impaired Skeletal Muscle Regeneration Induced by Macrophage Depletion Could Be Partly Ameliorated by MGF Injection. Front Physiol. 2019 May 17;10:601. https://pubmed.ncbi.nlm.nih.gov/31164836/ Doroudian G, Pinney J, Ayala P, Los T, Desai TA, Russell B. Sustained delivery of MGF peptide from microrods attracts stem cells and reduces apoptosis of myocytes. Biomed Microdevices. 2014 Oct;16(5):705-15. https://pubmed.ncbi.nlm.nih.gov/24908137/ Deng M, Zhang B, Wang K, Liu F, Xiao H, Zhao J, Liu P, Li Y, Lin F, Wang Y. Mechano growth factor E peptide promotes osteoblasts proliferation and bone-defect healing in rabbits. Int Orthop. 2011 Jul;35(7):1099-106. https://pubmed.ncbi.nlm.nih.gov/21057789/ Alec Walker. Hearts and Minds of Mice and Men: Mechano Growth Factor a new tool in the battle against age-related neuron loss? 20 Jul 2017. Kandalla PK, Goldspink G, Butler-Browne G, Mouly V. Mechano Growth Factor E peptide (MGF-E), derived from an isoform of IGF-1, activates human muscle progenitor cells and induces an increase in their fusion potential at different ages. Mech Ageing Dev. 2011 Apr. https://pubmed.ncbi.nlm.nih.gov/21354439/ Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
GHK-Cu (200mg)
GHK-Cu is a naturally occurring complex molecule composed of a tripeptide called GHK (made up of glycine, histidine, and lysine amino acids) bound to a copper ion. The copper ion appears to stabilize and deliver GHK to cells. Research suggests that GHK-Cu may play a potentially essential role in restoring damaged tissues, wound repair, and may support immune response. These hypotheses have sprung from it’s perceived potential to stimulate the production of collagen, elastin, and glycosaminoglycans, crucial intercellular matrix components. In addition to its potential on the intercellular matrix, GHK-Cu may also have antioxidant and anti-inflammatory characteristics that may protect cells from damage caused by free radicals. Chemical Makeup Molecular Formula: C14H23CuN6O4 Molecular Weight: 340.38 g/mol Other Known Titles: Cu-GHK, Copper tripeptide-1, 6BJQ43T1I9 Research and Clinical Studies GHK-Cu and Collagen Synthesis Studies suggest that GHK-Cu may stimulate collagen synthesis and induce in situ tissue recovery. The researchers suggest that these actions may be due to “the presence of a GHK triplet in the alpha 2(I) chain of type I collagen”.(1) More specifically, the tripeptide sequence composed of glycine, histidine, and lysine, abbreviated as Gly-His-Lys, may be derived during the breakdown of collagen through hydrolysis. This breakdown is typically associated with the disintegration of collagen fibers, frequently resulting from either tissue damage or the natural degradation process. It is proposed that this specific peptide sequence may have a significant impact on cellular communication processes, specifically targeting fibroblasts. Fibroblasts are specialized cells deemed essential in producing new collagen fibers, vital components for structural support in various tissues. The interaction between the Gly-His-Lys peptide and fibroblasts is believed to potentially initiate a cascade of biological events leading to the synthesis of collagen, thereby playing a potential role in the mechanisms of tissue repair and regeneration. This process of collagen synthesis by fibroblasts may be critical to contribute to the overall restoration and healing of damaged tissues. One study, lasted a month, reported that GHK-Cu might stimulate type 1 collagen production in clinical settings.(2) The scientists compared the potential of GHK-Cu to other peptides and vitamin C and vitamin A derivatives on photodamaged skin. The research primarily investigated the potential action of the peptide on dermal procollagen synthesis, keratinocyte proliferation, differentiation, and cutaneous inflammation. The peptide appeared to improve all indicators, and the researchers reported an apparent increase in skin thickness, elasticity, and hydration. Another study explored the potential interaction between GHK-Cu and hyaluronic acid (HA) on collagen synthesis, particularly focusing on their potential collaborative actions in dermal fibroblasts and an ex-vivo skin model.(3) HA is portrayed as a significant component of skin cells, noted for its moisture-binding potential and actions on cell proliferation and inflammation, with different molecular weights (LMW and HMW) showing distinct biological activities. The experimental setup involved exposure of dermal fibroblasts with various combinations of GHK-Cu and HA, measuring the synthesis of collagen types I, IV, and VII. It was suggested that certain combinations, particularly at a GHK-Cu to LMW HA ratio of 1:9, appeared to have significantly boosted the synthesis of collagen IV—more so than when either compound was studied independently. This suggests a potential synergistic action between GHK-Cu and HA, specifically in enhancing collagen IV levels. The synergy might arise from the combined action of GHK-Cu in stimulating glycosaminoglycan production, promoting collagen synthesis, and HA's role in reducing collagen degradation by scavenging reactive oxygen species and inhibiting matrix metalloproteinases. The research highlights that the molecular weight of HA and the ratio of GHK-Cu to HA may be crucial in maximizing this action, with optimal results observed at specific ratios. Further studies employing an ex-vivo skin model supported these findings, suggesting a notable increase in collagen IV synthesis at the dermal-epidermal junction when exposed to the optimized GHK-Cu and LMW HA mixture. This action was visually corroborated through increased fluorescence intensity in immunofluorescence assays, indicating higher collagen IV content. GHK-Cu and Wound Infection Both animal and clinical studies have hypothesized that GHK-Cu may reduce inflammation and the risk of infection in wounds. One murine study investigated the potential of GHK-Cu on ischemic open wounds.(4) The researchers reported, "On days 6, 10, and 13, tripeptide-copper complex-treated wounds contained significantly lower concentrations of TNF-alpha and MMP-2 and MMP-9 than control wounds.” Tumor necrosis factor-alpha (TNF-alpha), a cytokine involved in systemic inflammation, along with matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) — enzymes that break down extracellular matrix proteins — might potentially influence both the inflammatory processes and the remodeling of tissues. This suggests that GHK-Cu, a copper complex recognized for its healing capacities, might have a role in reducing inflammation and preventing tissue breakdown in models of ischemic wounds, where blood flow restriction potentially causes tissue damage. A clinical trial that involved GHK-Cu in addition to standard wound care also reported an apparently reduced risk of infection compared to standard processes alone.(5) The study was conducted on models of diabetic neuropathic ulcers, and the rate of infections was only 7% in the GHK-Cu models compared to 34% in the control models. GHK-Cu and Wound Healing Studies in rabbits report that GHK-Cu has been tested regarding its potential in wound healing and laser exposure at different intensities.(6) The results were compared to control wounds without intervention. Wounds were observed daily, and biopsies were taken weekly for four weeks to evaluate the inflammation rate and neovascularization. The GHK-Cu and high-intensity laser groups appeared to have a shorter average time for healing and greater neutrophil and vessel counts. There was an apparently shorter median time for the first observable granulation tissue and an apparently faster filling of an open wound with granulation tissue compared to the control group. Granular tissue is composed of newly formed connective tissue and minuscule blood vessels that appear on wound surfaces as part of the healing process. It is suggested that there might be a link between the emergence of this tissue and heightened activity of antioxidant enzymes. These enzymes are proteins that assist in shielding cells from the harmful action of oxidative stress, a process where cell components are damaged due to the presence of unstable molecules known as free radicals. Furthermore, there is a potential enhancement in vascular development observed in these scenarios. This vascular development is considered vital for transporting essential nutrients and oxygen to the damaged area, thereby facilitating the repair of tissue. The previously mentioned study on rats with open ischemic wounds also reported an apparent decrease in wound area of the GHK-Cu group that was greater compared to the control group on days 3 to 5, 6 to 9, and 11 to 13.(4) Similarly, the clinical study on models of diabetic neuropathic ulcers reported that GHK-Cu, combined with standard wound care, appeared more impactful for wound closure than standard care alone.(5) The apparent closure rate was three times faster than standard care. The researchers also suggested that “The enhancement of wound closure was more pronounced (median of 89.2% compared with -10.3% for vehicle; p < 0.01) in larger (greater than 100 mm(2) initial area at study entry) plantar ulcers caused by the failure of this size of ulcer to respond adequately to standardized wound care.” In research involving both standard murine models and those adapted to mimic diabetic conditions, wound dressings composed of collagen and infused with GHK were observed to potentially enhance wound healing.(7) The observations suggest that by the conclusion of the third week, wounds exposed to dressings containing biotinylated GHK (a tripeptide with skin regenerative properties) nearly achieved full closure, registering at 99.39%. This is potentially a significant enhancement compared to the 69.49% closure rate observed with control dressings lacking this modification. Further analysis indicated that the wounds exposed to GHK might have shown elevated levels of glutathione and ascorbic acid. These are considered critical antioxidants for their potential roles in facilitating tissue repair by protecting cells from oxidative stress. There was also a tentative observation of increased epithelialization, a process essential for the regeneration of the skin's outer layer, in these experimental conditions. Apart from the enhanced activity of fibroblasts, which are pivotal in collagen synthesis, tissue repair, and regeneration, there was also noted a potential rise in mast cell activation. Mast cells are important for mediating inflammatory responses, which are deemed crucial during the initial phases of wound healing. GHK-Cu and Active Radicals Photodamage of tissues such as the skin involves the formation of reactive oxygen species (ROS), reactive nitrogen species (RNS), and reactive carbonyl species (RCS), which may induce damage to proteins, DNA, and lipids. Studies suggest that the amino acid sequence in GHK-Cu may have anti-RCS potential against radicals such as 4-hydroxynoneal, acrolein, malondialdehyde, and others.(8) Furthermore, it may potentially prevent protein glycation. Moreover, researchers have suggested that GHK-Cu may have potential action in reducing iron release from ferritin. Ferritin is a lipid peroxidation catalyst, and GHK-Cu may help to reduce the formation of iron complexes in damaged tissues and thus decrease inflammation. One study suggested an 87% decrease in iron release with the help of GHK-Cu to lower oxidation in damaged tissues.(9) GHK-Cu may also reduce the production of reactive oxygen species and inflammatory cytokines while increasing the activity of antioxidant enzymes. This was proposed by an animal study investigating the potential of GHK-Cu on lipopolysaccharide-induced lung inflammation in mice.(10) The peptide was suggested to suppress the activation of NF-κB and p38 MAPK signaling pathways associated with inflammation. This might potentially lead to reduced infiltration of inflammatory cells in the lungs of mice with lung damage and lower levels of TNF-1 and IL-6 production to minimize damage. Further studies also suggest that the amino-acid sequence of GHK-Cu may have an antioxidative potential on ROS, such as hydroxyl radicals, and it may be even stronger than generic antioxidative peptides.(12) GHK-Cu and Wrinkles in Skin Tissue Models GHK-Cu has been suggested to host potential for improving experimental models of disturbed skin topography, such as wrinkles and fine lines. One study posited that a GHK-Cu possibly reduces visible bioindicators, improving skin laxity, and clarity. The peptide apparently also reduced the depth of wrinkles while potentially increasing skin density and thickness after 12 weeks of experimentation in skin cell models with varying degrees of photodamage.(13) Another investigation focused on the actions of GHK-Cu compared to a control compound and vitamin K. Over a period of 12 weeks, the GHK-Cu ostensibly performed better than the controls in reducing epidermal wrinkles. The peptide may also have increased skin density and thickness.(14) In a separate 12-week study in mild to advanced photodamage, GHK-Cu seemingly improved skin attributes such as laxity, clarity, and firmness. This peptide was also associated with a reduction in coarse wrinkles, and mottled pigmentation. Additionally, the peptide apparently stimulated dermal keratinocyte proliferation, as evidenced by histological analysis of biopsies.(15) GHK-Cu peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References Maquart, F. X., Pickart, L., Laurent, M., Gillery, P., Monboisse, J. C., & Borel, J. P. (1988). Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. FEBS letters, 238(2), 343–346. https://doi.org/10.1016/0014-5793(88)80509-x Abdulghani, A. A., Sherr, A., Shirin, S., Solodkina, G., Tapia, E. M., Wolf, B., & Gottlieb, A. B. (1998). Effects of creams containing vitamin C, a copper-binding peptide cream and melatonin compared with tretinoin on the ultrastructure of normal skin-A pilot clinical, histologic, and ultrastructural study. Disease Management and Clinical Outcomes, 4(1), 136-141. Jiang F, Wu Y, Liu Z, Hong M, Huang Y. Synergy of GHK-Cu and hyaluronic acid on collagen IV upregulation via fibroblast and ex-vivo skin tests. J Cosmet Dermatol. 2023 Sep;22(9):2598-2604. doi: 10.1111/jocd.15763. Epub 2023 Apr 16. PMID: 37062921. Canapp, S. O., Jr, Farese, J. P., Schultz, G. S., Gowda, S., Ishak, A. M., Swaim, S. F., Vangilder, J., Lee-Ambrose, L., & Martin, F. G. (2003). The effect of tripeptide-copper complex on healing of ischemic open wounds. Veterinary surgery : VS, 32(6), 515–523. https://doi.org/10.1111/j.1532-950x.2003.00515.x Mulder, G. D., Patt, L. M., Sanders, L., Rosenstock, J., Altman, M. I., Hanley, M. E., & Duncan, G. W. (1994). Enhanced healing of ulcers in patients with diabetes by treatment with glycyl-l-histidyl-l-lysine copper. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society, 2(4), 259–269. https://doi.org/10.1046/j.1524-475X.1994.20406.x Gul, N. Y., Topal, A., Cangul, I. T., & Yanik, K. (2008). The effects of tripeptide copper complex and helium-neon laser on wound healing in rabbits. Veterinary dermatology, 19(1), 7–14. https://doi.org/10.1111/j.1365-3164.2007.00647.x Alven, S., Peter, S., Mbese, Z., & Aderibigbe, B. A. (2022). Polymer-Based Wound Dressing Materials Loaded with Bioactive Agents: Potential Materials for the Treatment of Diabetic Wounds. Polymers, 14(4), 724. https://doi.org/10.3390/polym14040724 Cebrián, J., Messeguer, A., Facino, R. M., & García Antón, J. M. (2005). New anti-RNS and -RCS products for cosmetic treatment. International journal of cosmetic science, 27(5), 271–278. https://doi.org/10.1111/j.1467-2494.2005.00279.x Miller, D. M., DeSilva, D., Pickart, L., & Aust, S. D. (1990). Effects of glycyl-histidyl-lysyl chelated Cu(II) on ferritin dependent lipid peroxidation. Advances in experimental medicine and biology, 264, 79–84. https://doi.org/10.1007/978-1-4684-5730-8_11 Park, J. R., Lee, H., Kim, S. I., & Yang, S. R. (2016). The tri-peptide GHK-Cu complex ameliorates lipopolysaccharide-induced acute lung injury in mice. Oncotarget, 7(36), 58405–58417. https://doi.org/10.18632/oncotarget.11168 Zhang, Q., Yan, L., Lu, J., & Zhou, X. (2022). Glycyl-L-histidyl-L-lysine-Cu2+ attenuates cigarette smoke-induced pulmonary emphysema and inflammation by reducing oxidative stress pathway. Frontiers in molecular biosciences, 9, 925700. https://doi.org/10.3389/fmolb.2022.925700 Sakuma, S., Ishimura, M., Yuba, Y., Itoh, Y., & Fujimoto, Y. (2018). The peptide glycyl-ʟ-histidyl-ʟ-lysine is an endogenous antioxidant in living organisms, possibly by diminishing hydroxyl and peroxyl radicals. International journal of physiology, pathophysiology and pharmacology, 10(3), 132–138. Leyden J., Stephens T., Finkey M., Appa Y., Barkovic S. Skin care benefits of copper peptide containing facial cream. Proceedings of the American Academy of Dermatology Meeting; February 2002; New York, NY, USA. Leyden J., Stephens T., Finkey M., Barkovic S. Skin Care Benefits of Copper Peptide Containing Eye Creams. University of Pennsylvania; 2002. Finkley M., Appa Y., Bhandarkar S. Copper peptide and skin. In: Elsner P., Maibach H., editors. Cosmeceuticals and Active Cosmetics: Drugs vs. Cosmetics. New York, NY, USA: Marcel Dekker; 2005. pp. 549–563. Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
Adipotide (FTPP) (10mg)
Adipotide Peptide, also known as FTPP (Fat-Targeted Proapoptotic Peptide), fat-targeted proapoptotic peptide, or proapoptotic peptide, has been widely researched and is posited by scientists to be a proapoptotic peptide that may contribute to cell apoptosis. Adipotide may possibly act as a peptide targeting prohibitin, which is why it also bears the name Prohibitin-targeting peptide 1 (Prohibitin-TP01). Current research is still exploring Adipotide’s potential in this area and its potential actions related to its targeting properties.(1) Prohibitins are natural proteins considered by scientists to regulate such functions as cell formation, metabolism, and inflammation. Research teams initially considered Adipotide for its supposed potential to mitigate the action of cancer cells. Still, the peptide indicated it may have research potential for experiments investigating lipolysis and obesity mitigation, leaving the research pioneers “at a loss of words.”(2) It was presumed that Adipotide might prevent blood supply to the cancer cells, resulting in cell death and malignant cell growth inhibition. Upon further research, it was suggested by the scientists that the peptide appeared to exhibit the same mechanism of action but on fat cells instead. This “proof of concept” study was an early-stage experiment suggesting that the peptide may have significant potential. Yet, the compound has to be studied further to understand its full potential and impact on cells. Overview Researchers isolated a naturally occurring peptide (sequence CKGGRAKDC) via phage display methodology and combined it with a proapoptotic sequence, forming the now-termed Adipotide compound. Adipotide is homologous to the peptide sequence found in the white adipose tissue. Owing to this development and characteristics, researchers suggest that the peptide may possibly target the prohibitin PHB1 found at the surface of the adipose tissue – possibly attaching and thereby damaging them, potentially causing a blood supply disruption to the adipocytes (fat cells).(1) Prohibitins are considered by scientists to act as a vascular marker of the fatty tissues, and Adipotide may possibly be able to identify these markers and consequently conduct apoptosis on these cells.(3) Further, researchers speculate that Adipotide may interact not only with prohibitin but also another receptor called annexin A2 (ANX2) and thus potentially disrupt their role in supporting blood and fat supply to fat cells in white adipose tissue. Studies suggest that prohibitin and ANX2, when interacting in a complex with a fatty acid transporter called CD36, potentially facilitate the uptake of fatty acids by the endothelium and their subsequent transport into adipocytes. One study suggested that there was a purported white adipose tissue hypotrophy in murine models lacking ANX2, despite apparently normal white adipose tissue vascularization, adipogenesis, and glucose metabolism. This condition was potentially attributed to reduced fatty acid uptake by white adipose tissue endothelium and adipocytes. It was suggested that the efficiency of fatty acid transport relies on the interaction of ANX2 and prohibitin. This interaction was posited to be essential for mediating fatty acid transport from the endothelium into adipocytes. Additionally, it was commented that ANX2 and prohibitin form a complex with CD36, and this interaction is crucial for fatty acid transport. Importantly, the colocalization of prohibitin and CD36 on the adipocyte surface was induced by extracellular fatty acids, suggesting a dynamic regulation of this protein complex in response to fatty acid levels. The study posited that the biochemical interaction between ANX2 and prohibitin potentially regulates CD36-mediated fatty acid transport in white adipose tissue, unveiling a potential pathway that compounds like Adipotide might target.(4) Consequently, Adipotide is posited to potentially burn the fat stored in these fat cells as fuel, according to researchers' speculations.(2) Based on early preclinical studies on monkeys, it was also suggested that following Adipotide presentation, the monkeys exhibited apparently reduced insulin resistance.(5) Chemical Makeup Molecular Formula: C152H252N44O42 Molecular Weight: 2611.41 g/mol Other Known Titles: FTPP Research and Clinical Studies Adipotide (FTPP) Initial Research Adipotide's mode of action appears to hinge on its selective affinity for the receptor prohibitin, expressed on the surface of endothelial cells in the vasculature of white adipose tissue. The compound's potential to cause targeted apoptosis is facilitated by its fusion to the d-enantiomer D(KLAKLAK)2 sequence, an amphipathic peptidomimetic posited to disrupt mitochondrial membranes upon internalization into cells. This disruption might lead to cell death, specifically in the targeted vasculature. To evaluate the compound's potential, Adipotide was presented to three different types of primate models daily for four weeks. No deliberate changes were made to their diet or exercise routine. After the study, it was suggested by the researchers that the models apparently lost about 11% of weight and 39% of the fat deposits in their bodies compared to baseline.(5) As suggested by the authors, some of the models also exhibited apparent mild renal dysfunction, as reported across four study groups, A, B, C, and D. Creatinine levels apparently increased in study groups A and B, however, after a washout period, these returned to optimal levels. Further, the authors suggested that there may be an apparent reduction in food intake in the test models, which raises questions about potential actions on appetite or satiety signals, which could be another avenue through which Adipotide may exert its potential. However, the specific mechanisms by which Adipotide might influence these processes, if at all, are still unclear. While Adipotide is suggested to have potential at the cellular level for inducing weight loss by targeting the vasculature of white adipose tissue, its exact mechanisms of action, particularly in relation to appetite regulation and metabolic changes, require further investigation to fully understand its potential implications in the context of obesity. Adipotide (FTPP) and Malignant Cells Scientists surveyed a number of blood vessels and tissues (both normal and malignant), and isolated and studied the various peptides and molecules distributed in them. Peptides, proteins, and certain molecular distributions are considered to be specific and differentially expressed in normal and cancer tissues under control conditions. Through various chemical isolation and analytical techniques, researchers posited four native ligand receptors that appeared to be specific to certain types of carcinogenic cells. These receptors may, in turn, be vascular markets, and the researchers suggested that Adipotide exerts some of its potential action via these receptors. Notably, the research suggested four native ligand-receptors within the cells comprising the vasculature, two apparently common across multiple tissues and two potentially specific to certain tissues. The researchers posited common ligand-receptors were integrin α4/annexin A4 and cathepsin B/apolipoprotein E3. These were suggested following identification through protein purification, identification of native ligands from protein arrays, and supervised online database searches.(6) Adipotide (FTPP) and Diabetes In preliminary studies, obese murine models were given Adipotide to explore its potential mechanism on adipose cells. The research team noted it that within 2 to 3 days of the experiment, the murine models appeared to exhibit improved glucose tolerance and decreased levels of triglycerides.(7) More specifically, the study was conducted on obese murine models, and the alterations in glucose tolerance and metabolic variables were apparently observed without a corresponding change in body weight. This observation suggests a mechanism independent of weight loss. In the context of glucose homeostasis, Adipotide apparently improved glucose tolerance as suggested by a reduction in insulin and triglycerides, which was not merely a consequence of reduced food intake, as the changes differed from those in control groups with similar food intake. As noted, the apparent improvement in glucose tolerance was rapid, suggesting a potential direct influence of Adipotide on glucose regulatory mechanisms. Microarray analysis suggested shifts in gene expression within the white adipose tissue of Adipotide-presented murine models. Notably, pathways related to mitochondrial function, oxidative phosphorylation, and amino acid degradation appeared to be altered by the high-fat diet but were seemingly reversed by Adipotide. This suggests a potential role for Adipotide in modulating mitochondrial activity and metabolic processing in white adipose tissue, possibly contributing to improved glucose regulation. The study also explored the potential impact of Adipotide on various metabolic variables. While increased serum lipids were expected due to rapid white adipose tissue reduction, the findings were somewhat different. Triglycerides decreased in Adipotide-presented murine models, and there were distinctive levels of fatty acids and acylcarnitines compared to control groups. These observations hint at potential metabolic alterations not solely related to food intake or body weight changes. Another aspect examined was the serum levels of adipokines like adiponectin and resistin, which are considered to influence glucose regulation. The data did not suggest significant changes in these markers attributable to Adipotide, and the authors posited that the rapid improvement in glucose homeostasis might not be directly linked to these adipokines. Furthermore, Adipotide appeared to cause unique changes in serum acylcarnitines, indicating potential alterations in the mitochondrial metabolism of fatty acids and amino acids. Specifically, there was suggested to be a decrease in short- and medium-chain acylcarnitines and an increase in long-chain species, implying a shift in the metabolic processing of these molecules.(7) Adipotide peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Thuaud, F., Ribeiro, N., Nebigil, C. G., & Désaubry, L. (2013). Prohibitin ligands in cell death and survival: mode of action and therapeutic potential. Chemistry & biology, 20(3), 316–331. https://doi.org/10.1016/j.chembiol.2013.02.006 Melissa H., Cancer treatment shows promise for rapid weight loss, Los Angeles Times, 10 Nov 2011. https://www.latimes.com/local/la-xpm-2011-nov-10-la-he-drug-fat-loss-20111110-story.html Kolonin, Mikhail G et al. “Reversal of obesity by targeted ablation of adipose tissue.” Nature medicine vol. 10,6 (2004): 625-32. https://pubmed.ncbi.nlm.nih.gov/15133506/ Salameh A, Daquinag AC, Staquicini DI, An Z, Hajjar KA, Pasqualini R, Arap W, Kolonin MG. Prohibitin/annexin 2 interaction regulates fatty acid transport in adipose tissue. JCI Insight. 2016 Jul 7;1(10):e86351. doi: 10.1172/jci.insight.86351. PMID: 27468426; PMCID: PMC4959783. Barnhart, Kirstin F et al. “A peptidomimetic targeting white fat causes weight loss and improved insulin resistance in obese monkeys.” Science translational medicine vol. 3,108 (2011): 108ra112. doi:10.1126/scitranslmed.3002621. https://pubmed.ncbi.nlm.nih.gov/22072637/ Staquicini, Fernanda I et al. “Vascular ligand-receptor mapping by direct combinatorial selection in cancer patients.” Proceedings of the National Academy of Sciences of the United States of America vol. 108,46 (2011): 18637-42. doi:10.1073/pnas.1114503108. https://pubmed.ncbi.nlm.nih.gov/22049339/ Kim, Dong-Hoon et al. “Rapid and weight-independent improvement of glucose tolerance induced by a peptide designed to elicit apoptosis in adipose tissue endothelium.” Diabetes vol. 61,9 (2012): 2299-310. doi:10.2337/db11-1579. https://pubmed.ncbi.nlm.nih.gov/22733798/ Kolonin, Mikhail G et al. “Reversal of obesity by targeted ablation of adipose tissue.” Nature medicine vol. 10,6 (2004): 625-32. doi:10.1038/nm1048. https://pubmed.ncbi.nlm.nih.gov/15133506/ Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
ABP-7 (10mg)
ABP-7 (actin binding peptide-7) is a heptapeptide made of seven amino acids, which bears the sequence Acetyl-LKKTETQ. This peptide appears to be an N-acylated 17-23 fragment from a bigger molecule, Thymosin Beta 4. Consequently, this fragment is also sometimes termed a TB-500 Fragment. ABP-7 is a synthetic peptide, produced via solid-phase peptide synthesis.(1) Some researchers consider its LKKTETQ sequence to be the central actin-binding domain in Thymosin Beta 4. Therefore, ABP-7 is expected to have similar potential actions regarding actin binding, as its Thymosin Beta 4 counterpart.(2) Thymosin Beta 4 is posited to function as an actin-binding protein, particularly through its domain ABP-7. This domain notably inhibits the polymerization of globular actin (G-actin) into filamentous actin (F-actin), a process termed actin sequestration. This inhibition may result in elevated levels of G-actin within the cell. Actin, a pivotal component of the cellular cytoskeleton, is considered to not only provide structural integrity but may also play an essential role in various cellular activities, including cell motility and shape alteration. The mechanism by which ABP-7 may potentially prevent the polymerization of G-actin into F-actin appears to involve the stabilization of actin in its monomeric form, thereby limiting its availability to form the polymeric filaments necessary for a functional cytoskeleton. This alteration in the cytoskeletal architecture may impact the cell's ability to migrate and adapt its shape, which are considered to be critical functions in numerous biological processes. For instance, studies in wound healing and tissue regeneration suggest that cell motility may enable cells to move into and populate damaged areas to facilitate repair and restoration. Moreover, the possible disruption of actin polymerization by ABP-7 may influence other cellular mechanisms tied to actin dynamics, including intracellular transport and signal transduction pathways that rely on the actin cytoskeleton. The broader implications of these actions suggest that ABP-7's potential role in modulating actin polymerization could be significant in understanding and potentially manipulating cellular behaviors. Chemical Makeup Molecular Formula: C38H81N9O20 Molecular Weight: 889.5 g/mol Other Known Titles: TB-500 Fragment, Ac-LKKTETQ Research and Clinical Studies ABP-7 and Wounds One study aimed to evaluate the actions of ABP-7, considered the central actin-binding domain of Thymosin Beta 4 (Tb4), focusing on its role in promoting wound repair in aged murine models. The peptide's potential to enhance wound healing was assessed by examining parameters such as keratinocyte migration, collagen deposition, and wound closure.(3) More specifically, the researchers posited that “the actin-binding domain of thymosin beta 4 duplicated in a seven-amino acid synthetic peptide, LKKTETQ, was able to promote repair in the aged animals comparable to that observed with the parent molecule.” The study suggests that the ABP-7 peptide possibly promotes repair in aged murine models in ways that appear comparable to those observed with the parent molecule, Tb4. It is posited that the ABP-7 peptide may encourage epidermal cell migration and increase collagen deposition within the wound site. These activities suggest that the peptide might facilitate the closure and healing of wound models. Moreover, it is mentioned that Thymosin Beta 4 and its derived peptides, including ABP-7, have been studied in various contexts of wound healing and have been evaluated for their general potential in enhancing keratinocyte migration, a crucial aspect of the healing process. The ABP-7 peptide, by mimicking a specific functional domain of Tb4, possibly harnesses similar biological pathways to promote wound repair, although the study suggests that further research is needed to fully understand the peptide's mechanism of action and its potential applicability in this specific field of study. Studies have purported various mechanisms via which ABP-7 may speed up the healing of lesions and skin wounds.(4) One proposed mechanism suggests that ABP-7 may interact with purinergic receptors, which are considered to play pivotal roles in cellular responses to injury. The enhancement of wound healing observed in the presence of ABP-7 may be mediated by these receptors. The interaction may increase intracellular calcium levels, which is believed to be a critical factor in activating cellular pathways that facilitate wound closure. This rise in calcium levels might stimulate processes such as cell migration and extracellular matrix remodeling, which are essential for wound model repair. Additionally, the peptide’s interaction with actin—a fundamental component of the cellular cytoskeleton—suggests a mechanism where ABP-7 might influence actin dynamics. By binding to actin, ABP-7 might potentially stabilize or alter the structure of the cytoskeleton, thereby affecting the cell’s ability to migrate and cover the wound models. Furthermore, the possibility that ABP-7 enhances the activation of downstream signaling pathways, such as those mediated by MAP kinases, cannot be ruled out. These pathways are considered to often regulate gene expression related to cell proliferation and migration. The modulation of these pathways by ABP-7 might enhance the cellular responses necessary for wound healing. ABP-7 and Tissue Scarring (Fibrosis) Research has been undertaken to investigate the potential anti-fibrotic properties of ABP-7 and its actions on hepatic stellate cells (HSC) within the context of liver fibrosis. One study posits that ABP-7 might influence the behavior of these cells. Preliminary data tentatively suggests that ABP-7 might potentially inhibit the PDGF-BB-dependent up-regulation of critical biomarkers such as PDGFβ receptor, α-smooth muscle actin (α-SMA), and collagen type I. Furthermore, it appears that ABP-7 may obstruct the phosphorylation of Akt at both T308 and S473 sites, which might consequently impede the phosphorylation of PRAS40. In elaborating on these pathways, the PDGF-BB-dependent up-regulation is believed to involve an enhancement of specific cellular signals initiated by PDGF-BB, a platelet-derived growth factor that engages and activates the PDGFβ receptor. The scientists commented that the fragment may have “prevented the PDGF-BB induced reappearance of the receptor protein once it is already degraded.”(5) This receptor is considered crucial for cellular growth and division. α-Smooth muscle actin (α-SMA), serves as a marker for the transition of quiescent stellate cells into their contractile phenotype, considered a critical event in the development of fibrosis. Collagen type I is a principal component of the extracellular matrix that tends to accumulate during liver fibrosis. Regarding the signaling aspect, the phosphorylation of Akt at the T308 and S473 sites is hypothesized to activate Akt, potentially leading to the activation of several downstream proteins, including PRAS40, lauded as an essential regulator of cell survival and metabolism. The inhibition of these phosphorylation events may, theoretically, disrupt these signaling pathways, which are believed to be vital for the integral processes of cell proliferation and migration in fibrogenesis. This inhibition sequence is conjectured to correlate with a reduction in the proliferation and migration of activated HSCs. These observations suggest that ABP-7 may possibly play an influential role in mitigating the activation of HSC and the subsequent fibrotic response.(5) ABP-7 and Angiogenesis The peptide ABP-7 may have a role in promoting angiogenesis, or the development of new blood vessels. It is thought that ABP-7 might facilitate endothelial cell behaviors crucial for new blood vessel formation, such as migration and tube formation in vitro. These processes are considered essential for angiogenesis, where endothelial cells may migrate, align, and form tubular structures to establish new blood vessels. Ex vivo assays, such as sprouting from aortic rings, have suggested that ABP-7 may possibly support the initial steps of vessel sprouting.(2) Researchers consider vessel sprouting as a potential step in angiogenesis. The addition of ABP-7 to these systems might indicate reduced interaction of actin with other cellular components by its actin-binding activity, thus potentially freeing up actin to participate more actively in the dynamic structural changes that endothelial cells undergo during angiogenesis. It is posited that by modifying actin's availability or organization within endothelial cells, ABP-7 might be influencing the cellular architecture in a way that favors angiogenic processes. This may involve cell shape and motility alterations, which are critical for forming new vascular structures. Given the complexity of angiogenic signaling and the multiple steps involved, it is also possible that ABP-7 may interact indirectly with other cellular pathways or signaling molecules that contribute to angiogenesis. These potential interactions and their actions on angiogenesis are still under investigation and hold the promise for further elucidation in future studies. ABP-7 peptide is available for research and laboratory purposes only. Please review our Terms and Conditions before ordering. References: Esposito, S., Deventer, K., Goeman, J., Van der Eycken, J., & Van Eenoo, P. (2012). Synthesis and characterization of the N-terminal acetylated 17-23 fragment of thymosin beta 4 identified in TB-500, a product suspected to possess doping potential. Drug testing and analysis, 4(9), 733–738. https://doi.org/10.1002/dta.1402 Sosne, G., Qiu, P., Goldstein, A. L., & Wheater, M. (2010). Biological activities of thymosin beta4 defined by active sites in short peptide sequences. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 24(7), 2144–2151. https://doi.org/10.1096/fj.09-142307 Philp, D., Badamchian, M., Scheremeta, B., Nguyen, M., Goldstein, A. L., & Kleinman, H. K. (2003). Thymosin beta 4 and a synthetic peptide containing its actin-binding domain promote dermal wound repair in db/db diabetic mice and in aged mice. Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society, 11(1), 19–24. https://doi.org/10.1046/j.1524-475x.2003.11105.x Huang, C. M., Wang, C. C., Barnes, S., & Elmets, C. A. (2006). In vivo detection of secreted proteins from wounded skin using capillary ultrafiltration probes and mass spectrometric proteomics. Proteomics, 6(21), 5805–5814. https://doi.org/10.1002/pmic.200600163 Shah, R., Reyes-Gordillo, K., & Rojkind, M. (2018). Thymosin β4 inhibits PDGF-BB induced activation, proliferation, and migration of human hepatic stellate cells via its actin-binding domain. Expert opinion on biological therapy, 18(sup1), 177–184. https://doi.org/10.1080/14712598.2018.1478961 { "@context": "https:\/\/schema.org", "@type": "Product", "name": "ABP-7 (10mg)", "description": "ABP-7 for sale online (10mg). Peptides for sale at 99% purity with top customer service. Get research study results and information.", "image": "https://www.painandanxietymeds.shop/wp-content/uploads/2024/05/ABP-7-10mg-300x300.jpg", "offers": [ { "@type": "Offer", "priceCurrency": "USD", "price": 92, "availability": "https:\/\/schema.org\/InStock", "itemCondition": "https:\/\/schema.org\/NewCondition", "seller": { "@type": "Organization", "name": "painandanxietymeds.shop" }, "url": "https:\/\/www.painandanxietymeds.shop\/abp-7-10mg/", "hasMerchantReturnPolicy": { "@type": "MerchantReturnPolicy", "applicableCountry": "US", "returnPolicyCategory": "https:\/\/schema.org\/MerchantReturnNotPermitted" }, "shippingDetails": { "@type": "OfferShippingDetails", "shippingRate": { "@type": "MonetaryAmount", "minValue": 0, "maxValue": 9.25, "currency": "USD" }, "shippingDestination": { "@type": "DefinedRegion", "addressCountry": "US" }, "deliveryTime": { "@type": "ShippingDeliveryTime", "handlingTime": { "@type": "QuantitativeValue", "minValue": 1, "maxValue": 2, "unitCode": "d" }, "transitTime": { "@type": "QuantitativeValue", "minValue": 1, "maxValue": 5, "unitCode": "d" } } }, "priceValidUntil": "2027-04-04T15:10:59+00:00" } ], "url": "https:\/\/www.painandanxietymeds.shop\/abp-7-10mg/", "aggregateRating": { "@type": "AggregateRating", "ratingValue": 98, "bestRating": 100, "reviewCount": 152 }, "review": [] } Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
Mod GRF 1-29 & GHRP-6 Blend (10mg)
GHRP-6 (Growth Hormone Releasing Peptide-6) is a synthetic peptide developed to stimulate the release of growth hormone from the pituitary gland by mimicking the effects of ghrelin. It is classified as ghrelin mimetic or GHS (growth hormone secretagogue). It is composed of six amino acids and is classified as a hexapeptide. GHRP-6 has been studied to explore its potential action, which includes possible mitigation of growth hormone deficiency and cachexia (muscle wasting).(1) Modified (Mod) GRF 1-29, also known as CJC-1295 without DAC (Drug Affinity Complex), is a synthetic peptide developed to act as a growth hormone-releasing hormone (GHRH) analog. It comprises 29 amino acids and is a tetrasubstituted version of the GRF 1-29 (Growth-Releasing Factor). GRF 1-29 is the smallest fragment of the GHRH peptide sequence, which may have the same potential for stimulating growth hormone release. Chemical Makeup Molecular Formula: Mod GRF 1-29: C152H252N44O42 GHRP-6: C46H56N12O6 Molecular Weight: Mod GRF 1-29: 3367.95 g/mol GHRP-6: 873.03 g/mol Other Known Titles Mod GRF 1-29: CJC-1295 NO DAC; tetrasubstituted GRF 1-29 GHRP-6: Growth Hormone Releasing Peptide-6 Research and Clinical Studies Mod GRF 1-29 & GHRP-6 Peptide and the Pituitary Mod GRF 1-29 and GHRP-6 has been suggested by researchers to work to upregulate growth hormone and insulin-like growth factor-1 (IGF-1) by activating the GHRH-receptors and the ghrelin receptors, respectively.(2) Mod GRF 1-29 appears to bind to the GHRH receptors on somatotroph cells in the anterior pituitary gland. It is hypothesized that this binding might be a potential trigger for subsequent intracellular events that possibly lead to growth hormone release. Upon binding to the receptors, Mod GRF 1-29 may potentially initiate a series of intracellular signaling cascades.(2) One pathway that appears to be activated is the adenylyl cyclase pathway, which might lead to the conversion of ATP (adenosine triphosphate) into cAMP (cyclic adenosine monophosphate). The rise in cAMP levels may possibly activate protein kinase A (PKA). This activation may result in the phosphorylation of various proteins, including the voltage-dependent calcium channels on the cell membrane. It is posited that the phosphorylation and potential opening of these calcium channels allow calcium ions to flow into the somatotropic cells. Elevated intracellular calcium concentrations are believed to play a role in subsequent steps of growth hormone release. It has also been hypothesized that high intracellular calcium concentrations may stimulate the secretory vesicles within the somatotroph cells to release growth hormone into the circulation. On the other hand, GHRP-6 has been suggested by researchers to bind to and potentially activate the ghrelin receptor, known as GHS-R1a (Growth Hormone Secretagogue Receptor 1a), which might hypothetically cause the release of growth hormone. GHRP-6 is believed to be a synthetic hexapeptide that may have a high affinity for the GHS-R1a.(3) Upon binding, GHRP-6 appears to induce a hypothetical conformational change, potentially activating the receptor. The apparent binding of GHRP-6 to GHS-R1a might activate several intracellular signaling pathways. One pathway that seems to be activated is the phospholipase C (PLC) pathway, which might lead to the production of inositol trisphosphate (IP3) and diacylglycerol (DAG). IP3 which then may initiate the release of calcium from intracellular stores, possibly leading to a rise in intracellular calcium levels. This increase in calcium is posited to play a role in the release of GH from the pituitary. Mod GRF 1-29 & GHRP-6 Peptide and Potential Synergism It is hypothesized that GHRP-6 may exert a synergistic effect when introduced alongside Mod GRF 1-29. While both GHRP-6 and Mod GRF 1-29 have been suggested to potentially stimulate GH release individually, their combined effect appears to be more significant than their individual impacts. This suggests that GHRP-6 and Mod GRF 1-29 might influence different somatotroph populations or that they may affect different phases of the growth hormone release process. Several studies suggest the existence of such synergisms. For example, one study reported an apparent increase in IGF-1 levels of over 65% after the combined introduction of GHRP-6 and the unmodified version of Mod GRF 1-29.(4) In comparison, previous research has suggested that Mod GRF 1-29 may potentially lead to a 27-28% increase in IGF-1, which is considerably lower increase.(5) A subsequent study appears to suggest that the original, possibly unaltered version of Mod GRF 1-29, which may be akin to native GHRH, potentially led to a 20-fold surge in pulsatile growth hormone release. At the same time, a GHRP that seems similar to GHRP-6 was apparently observed to cause a 47-fold rise in pulsatile growth hormone levels. Interestingly, when GHRH and GHRP were possibly combined, the mixture may have resulted in a 54-fold increase in pulsatile GH release compared to baseline, which may hint at a synergistic effect. This combination might, in theory, offer enhanced stimulation of growth hormone secretion.(6) Mod GRF 1-29 & GHRP-6 Peptide and Muscle Mass GHRP-6 and Mod GRF 1-29 have been suggested by researchers to exert anabolic properties by increasing growth hormone levels. For example, clinical studies with GRF 1-29 suggest that it may increase nocturnal growth hormone levels, serum levels of IGF-I and IGFBP-3, and GHBP concentrations.(5) As a result, male test subjects who were presented the peptide for four months reportedly experienced a significant increase in lean body mass by 1.26 kg. The peptide also appeared to induce a possible increase in skin thickness in male subjects and possible improved insulin sensitivity. Another trial supported the hypothesis that GRF (1-29) might increase GH and IGF-I levels and improve skeletal muscle function and metabolism in ambulatory, non-obese subjects aged 64 to 76 years with low baseline IGF-I.(7) More specifically, GRF (1-29) appeared to increase mean nocturnal GH release, GH peak amplitude, and two measures of muscle strength and a muscle endurance test. GHRP-6 also may have anabolic potential, according to certain study findings. This potential is likely mediated via its alleged growth hormone and IGF-1 stimulating action. One experiment with cultured myoblast cells reported that the peptide appeared to increase the expression of myogenic marker proteins, insulin-like growth factor-1, collagen type I, and metabolic activity in the myoblasts.(8) Thus, the scientists concluded that the peptide GHRP-6 might improve muscle condition by stimulating collagen type I synthesis and key proteins. Mod GRF 1-29 & GHRP-6 Peptide and Growth Hormone Deficiency GRF 1-29 and GHRP-6 have been investigated for their potential to stimulate growth in models of growth hormone deficiencies. One clinical study investigated the potential of GRF 1-29 for growth hormone deficiency.(9) In total, 110 subjects were presented with the peptide once daily for up to one year, and the main outcomes measured were linear growth enhancement and bone age progression. The peptide appeared to exhibit a significant increase in height velocity, with 74% of the subjects having a reportedly enhanced response after six months. The bone age to height age ratio was reported to remain stable. The researchers concluded, “No change in fasting glucose concentration or excessive generation of insulin-like growth factor I occurred, and overall GHRH was well tolerated.” Another clinical trial aimed to investigate the potential of GHRP-6 in stimulating growth hormone (GH) secretion in subjects with normal height.(10) The study included 13 subjects, and the results suggested that the GH response to GHRP-6 was reportedly significant and comparable to that of other GHSs. Mod GRF 1-29 & GHRP-6 Peptide and Wasting, Cachexia Mod GRF 1-29 and GHRP-6 reportedly exhibits some potential to increase growth hormone and IGF-1 levels, which may have anti-catabolic actions on muscle tissue. For example, GRF 1-29 was suggested to significantly increase growth hormone peak levels in research models, even though the potential appeared slightly attenuated in those with growth hormone deficiency.(11) Despite no direct research on Mod GRF 1-29 (without DAC), studies on Mod GRF 1-29 with DAC report apparently increased HGH and IGF-1 levels in the test subjects.(12) GHRP-6 may also cause a dramatic increase in growth hormone levels, according to researchers in clinical trials. For example, Cordido et al. suggested that GHRP-6 might increase GH secretion in 19 obese subjects.(13) The scientists noted that GHRP-6 appeared more impactful than GHRH alone, stating, “GH responses to GHRP-6 were almost twice those to GHRH in obese patients.” GHRP-6 was developed with the intention of having potential as a ghrelin mimetic. Studies suggest that mimetics have shown promise in reversing protein breakdown and weight loss in catabolic states.(14) Ghrelin has various potential actions on regulating appetite, body composition, growth hormone secretion, and energy expenditure. It may also have anti-inflammatory, anti-apoptotic, and anxiolytic potential as well. Mod GRF 1-29 & GHRP-6 peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Cabrales, A., Gil, J., Fernández, E., Valenzuela, C., Hernández, F., García, I., Hernández, A., Besada, V., Reyes, O., Padrón, G., Berlanga, J., Guillén, G., & González, L. J. (2013). Pharmacokinetic study of Growth Hormone-Releasing Peptide 6 (GHRP-6) in nine healthy male volunteers. European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 48(1-2), 40–46. https://doi.org/10.1016/j.ejps.2012.10.006 Sinha, D. K., Balasubramanian, A., Tatem, A. J., Rivera-Mirabal, J., Yu, J., Kovac, J., Pastuszak, A. W., & Lipshultz, L. I. (2020). Beyond the androgen receptor: the role of growth hormone secretagogues in the modern management of body composition in hypogonadal males. Translational andrology and urology, 9(Suppl 2), S149–S159. https://doi.org/10.21037/tau.2019.11.30 Abizaid, A., & Hougland, J. L. (2020). Ghrelin Signaling: GOAT and GHS-R1a Take a LEAP in Complexity. Trends in endocrinology and metabolism: TEM, 31(2), 107–117. https://doi.org/10.1016/j.tem.2019.09.006 Sigalos, J. T., Pastuszak, A. W., Allison, A., Ohlander, S. J., Herati, A., Lindgren, M. C., & Lipshultz, L. I. (2017). Growth Hormone Secretagogue Treatment in Hypogonadal Men Raises Serum Insulin-Like Growth Factor-1 Levels. American journal of men's health, 11(6), 1752–1757. https://doi.org/10.1177/1557988317718662 Khorram, O., Laughlin, G. A., & Yen, S. S. (1997). Endocrine and metabolic effects of long-term administration of [Nle27]growth hormone-releasing hormone-(1-29)-NH2 in age-advanced men and women. The Journal of clinical endocrinology and metabolism, 82(5), 1472–1479. https://doi.org/10.1210/jcem.82.5.3943 Veldhuis, J. D., & Keenan, D. M. (2008). Secretagogues govern GH secretory-burst waveform and mass in healthy eugonadal and short-term hypogonadal men. European journal of endocrinology, 159(5), 547–554. https://doi.org/10.1530/EJE-08-0414 Vittone, J., Blackman, M. R., Busby-Whitehead, J., Tsiao, C., Stewart, K. J., Tobin, J., Stevens, T., Bellantoni, M. F., Rogers, M. A., Baumann, G., Roth, J., Harman, S. M., & Spencer, R. G. (1997). Effects of single nightly injections of growth hormone-releasing hormone (GHRH 1-29) in healthy elderly men. Metabolism: clinical and experimental, 46(1), 89–96. https://doi.org/10.1016/s0026-0495(97)90174-8 Lim, C. J., Jeon, J. E., Jeong, S. K., Yoon, S. J., Kwon, S. D., Lim, J., Park, K., Kim, D. Y., Ahn, J. K., & Kim, B. W. (2015). Growth hormone-releasing peptide-biotin conjugate stimulates myocytes differentiation through insulin-like growth factor-1 and collagen type I. BMB reports, 48(9), 501–506. https://doi.org/10.5483/bmbrep.2015.48.9.258 Thorner, M., Rochiccioli, P., Colle, M., Lanes, R., Grunt, J., Galazka, A., Landy, H., Eengrand, P., & Shah, S. (1996). Once daily subcutaneous growth hormone-releasing hormone therapy accelerates growth in growth hormone-deficient children during the first year of therapy. Geref International Study Group. The Journal of clinical endocrinology and metabolism, 81(3), 1189–1196. https://doi.org/10.1210/jcem.81.3.8772599 Bellone, J., Ghizzoni, L., Aimaretti, G., Volta, C., Boghen, M. F., Bernasconi, S., & Ghigo, E. (1995). Growth hormone-releasing effect of oral growth hormone-releasing peptide 6 (GHRP-6) administration in children with short stature. European journal of endocrinology, 133(4), 425–429. https://doi.org/10.1530/eje.0.1330425 Achermann, J. C., Hindmarsh, P. C., Robinson, I. C., Matthews, D. R., & Brook, C. G. (1999). The relative roles of continuous growth hormone-releasing hormone (GHRH(1-29)NH2) and intermittent somatostatin(1-14)(SS) in growth hormone (GH) pulse generation: studies in normal and post cranial irradiated individuals. Clinical endocrinology, 51(5), 575–585. https://doi.org/10.1046/j.1365-2265.1999.00839.x Teichman, S. L., Neale, A., Lawrence, B., Gagnon, C., Castaigne, J. P., & Frohman, L. A. (2006). Prolonged stimulation of growth hormone (GH) and insulin-like growth factor I secretion by CJC-1295, a long-acting analog of GH-releasing hormone, in healthy adults. The Journal of clinical endocrinology and metabolism, 91(3), 799–805. https://doi.org/10.1210/jc.2005-1536 Sigalos, J. T., & Pastuszak, A. W. (2018). The Safety and Efficacy of Growth Hormone Secretagogues. Sexual medicine reviews, 6(1), 45–53. https://doi.org/10.1016/j.sxmr.2017.02.004 Khatib, M. N., Gaidhane, A., Gaidhane, S., & Quazi, Z. S. (2018). Ghrelin as a Promising Therapeutic Option for Cancer Cachexia. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 48(5), 2172–2188. https://doi.org/10.1159/000492559 Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.