Medicines & Treatments
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.
SNAP-8 (200mg)
Synaptosomal-associated protein 8, or the SNAP-8 peptide, is a synthetic octapeptide analog of the N-terminal end of the SNAP-25 peptide. The peptide is made of eight amino acids. It is acetylated at the N-terminus and amidated at the C-terminus, which leads to the following structure: Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2. Overview This peptide was developed to compete with the SNAP-25 protein to bind with the vehicle-associated membrane proteins. The SNAP-25 protein, which stands for Synaptosomal-Associated Protein of 25 kDa, is considered a key component in neurotransmitter release. It normally interacts with vehicle-associated membrane proteins to facilitate the fusion of vesicles with the cell membrane, releasing their contents into the synaptic gap. Such a vesicle-associated membrane protein is thought to be synaptic vesicle protein Synaptotagmin 1 (Syt1). Synaptotagmin 1 (Syt1) serves as a calcium sensor and is deemed crucial for regulating neurotransmitter release in response to changes in calcium ion concentrations inside nerve cells. Molecular docking experiments posited that SNAP-8 and other peptides might bind to the C2A–C2B interface, primarily driven by hydrophobic contacts, suggesting a plausible site for inhibitory action on Syt1. The C2A and C2B regions are parts of the protein structure of Synaptotagmin 1 involved in calcium binding and membrane interaction. The binding at this interface by SNAP-8 suggests that the peptide might interfere with Synaptotagmin 1’s ability to respond to calcium signals, potentially disrupting normal neurotransmission. Once the SNAP-8 peptide binds with these proteins, it appears to destabilize the formation of the Soluble N-ethylmaleimide-sensitive factor Attachment Protein Receptor (SNARE) complex. The SNARE complex is instrumental in the docking and fusion of vesicles at the cell membrane. Destabilization of this complex may prevent the release of acetylcholine, reducing localized muscle contractions. Acetylcholine is a neurotransmitter involved in stimulating muscle contractions. Its reduced release may therefore lead to decreased muscle activity and reduced wrinkle depth. Ultimately, all these biological activities induced by SNAP-8 peptide may cause a reduction in lines and wrinkles.(1) Thus, the potential of SNAP-8 to interact at the molecular level with components of the neurotransmitter release mechanism showcases it may act as a modulator of neural and muscular function, specifically in experimental models of skin cell aging. Chemical Makeup(2) Molecular Formula: C41H70N16O6S Molecular Weight: 1075.16 g/mol Other Known Titles: SNAP-8 (Acetyl Glutamyl Heptapeptide-3), Synaptosomal-associated protein 8, Acetyl octapeptide-3 Research and Clinical Studies SNAP-8 Peptide and Skin Wrinkling A study(3) was conducted in 2021 to study the potential of the peptide on expression lines and wrinkles. In this double-blind, randomized clinical trial, 55 research models were observed. The entire cohort exhibited Fitzpatrick skin type I to VI, and were exposed either the peptide serum or a control compound twice a day for 12 weeks. Short-term peptide impact was measured 15 minutes after exposure, and long-term impact was measured at weeks 4, 8, and 12. After completing this study, it was observed that the peptide appeared to cause a notable reduction in the lines within 15 minutes after introduction. For long-term impact, it was suggested by the researchers that the peptide had the potential to induce significant skin improvement after 12 weeks. In another clinical trial conducted in 2013,(4) scientists focused on the Argireline peptide, a synthetic analog of the N-terminal end of the SNAP-25 peptide, which was developed for anti-aging action within the cell by inhibiting the catecholamine release (as opposed to acetylcholine release). Since both peptides are similar in structure, this study's results may reflect parallel actions of the SNAP-8 peptide. For this trial, 60 models were examined, of which 45 were presented with the peptide, and 15 were presented with a control compound. The peptide or the control was introduced every day for four weeks. After the completion of the study, it was reported that the peptide group appeared to have improved skin, with almost a 49% reduction in lines and decreased skin roughness. As per Yuan Wang et al.: "In the subjective evaluation, the total anti-wrinkle efficacy in the argireline group was 48.9%, compared with 0% in the placebo group. In the objective evaluation, the parameters of roughness were all decreased in the argireline group (p < 0.01), while no decrease was obvious in the placebo group (p > 0.05).” SNAP-8 Peptide and Skin Topography A study(5) aimed to evaluate whether the SNAP-8 peptide might be incorporated into an oil and water emulsion form to understand the peptide’s stability. When the 10% peptide oil-in-water emulsion was evaluated over a month-long routine exposure, there appeared to be a ~30% reduction in the depth and appearance of wrinkles. Researchers suggest that the peptide potentially mimics the action of botulinum neurotoxins.(6) SNAP-8 Peptide and SNARE Protein Complex SNAP-8 peptide has shown the potential to reduce muscle contractions by modulating the SNARE protein complex. One study reported that the peptide appeared to reduce the release of glutamate amino acid by almost 43%. Researchers reportedly claimed that the SNAP-8 peptide might reduce wrinkles by an average of 35%, up to a maximum of 62%,(7) a notable improvement in skin texture. SNAP-8 peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References Lim SH, Sun Y, Thiruvallur Madanagopal T, Rosa V, Kang L. Enhanced Skin Permeation of Anti-wrinkle Peptides via Molecular Modification. Sci Rep. 2018 Jan 25;8(1):1596. doi: 10.1038/s41598-017-18454-z. Erratum in: Sci Rep. 2018 Apr 20;8(1):6500. PMID: 29371611; PMCID: PMC5785486. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5785486/ National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 86080331, SNAP-8(Acetyl Glutamyl Heptapeptide-3). from https://pubchem.ncbi.nlm.nih.gov/compound/SNAP-8_Acetyl-Glutamyl-Heptapeptide-3 Nguyen TQ, Zahr AS, Kononov T, Ablon G. A Randomized, Double-blind, Placebo-controlled Clinical Study Investigating the Efficacy and Tolerability of a Peptide Serum Targeting Expression Lines. J Clin Aesthet Dermatol. 2021 May;14(5):14-21. Epub 2021 May 1. PMID: 34188744; PMCID: PMC8211334. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8211334/ Wang Y, Wang M, Xiao S, Pan P, Li P, Huo J. The anti-wrinkle efficacy of argireline, a synthetic hexapeptide, in Chinese subjects: a randomized, placebo-controlled study. Am J Clin Dermatol. 2013 Apr;14(2):147-53. doi: 10.1007/s40257-013-0009-9. PMID: 23417317. https://pubmed.ncbi.nlm.nih.gov/23417317/ Blanes-Mira C, Clemente J, Jodas G, Gil A, Fernández-Ballester G, Ponsati B, Gutierrez L, Pérez-Payá E, Ferrer-Montiel A. A synthetic hexapeptide (Argireline) with anti-wrinkle activity. Int J Cosmet Sci. 2002 Oct;24(5):303-10. doi: 10.1046/j.1467-2494.2002.00153.x. PMID: 18498523. https://pubmed.ncbi.nlm.nih.gov/18498523/ Apland JP, Adler M, Oyler GA. Inhibition of neurotransmitter release by peptides that mimic the N-terminal domain of SNAP-25. J Protein Chem. 2003 Feb;22(2):147-53. doi: 10.1023/a:1023423013741. PMID: 12760419. https://pubmed.ncbi.nlm.nih.gov/12760419/ Errante F, Ledwoń P, Latajka R, Rovero P, Papini AM. Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Front Chem. 2020 Oct 30;8:572923. doi: 10.3389/fchem.2020.572923. PMID: 33195061; PMCID: PMC7662462. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7662462/ Sadowski G, Sadowski J. Safety and Efficacy of a Novel Anti-aging Skin Care Regimen Containing Neutraceuticals and Growth Factors on the Facial Skin of Women: A 12-Week Open-label Study. J Clin Aesthet Dermatol. 2020 Jun;13(6):24-34. Epub 2020 Jun 1. PMID: 32884616; PMCID: PMC7442306. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7442306 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.
Testagen (20mg)
Testagen, alternatively known as KEDG, is classified among the Khavinson peptides and functions as a short signaling peptide. Short peptides such as Testagen are also suggested to serve as bioregulators which means that they may potentially cross both the cell and nuclear membranes to interact directly with DNA of target tissues.(1) Potentially, it may interact with the function of the anterior pituitary gland cells and interact with endocrine pathways that play a role in the synthesis of testosterone and thyroid-stimulating hormone (TSH).(2) This is likely due to the synthesis of Testagen, which is based on the amino acid composition of extracts from the anterior lobe of the pituitary gland.(3) As a result, it is made of the amino acids lysine, glutamine, asparagine and glycine, forming a tetrapeptide. Chemical Makeup Molecular formula: C17H29N5O9 Molecular weight: 447.2 g/mol Sequence: Lys-Glu-Asp-Gly Reconstitution: Required Other known titles: KEDG, Anterior pituitary peptide (APP) Research and Clinical Studies Testagen and the Hypothalamic-Pituitary-Gonadal Axis Testagen appears to be a bioregulator that may interact with the pituitary gland to upregulate testosterone production. Some trials suggest that the peptide may enhance testosterone production in research models of chronic inflammation and low testosterone as a result. Testagen was suggested to potentially improve uroflowmetry indicators, reduce markers of inflammation, and potentially cause an elevation in the total levels of testosterone. The researchers commented about “a decrease in the level of inflammation in the prostate, an increase in the level of total testosterone.”(4) While the exact mechanisms behind the potential of testagen remain unknown, some researchers have posited that the peptide may potentially have interactions with histones, which might influence epigenetic mechanisms, affecting cellular activities and differentiation. This interaction between short peptides and histones, particularly in the N-terminal histone regions containing seemingly homologous peptide-binding motifs, suggests an intriguing role in the regulation of chromatin structure and gene expression. Testagen has been observed to bind to certain histone regions with a specific conformational structure, this implies a potential impact on the structural dynamics of chromatin. Although core histones did not reveal homologous amino acid sequences, the specific binding indicates that peptides might interact with them through unique spatial conformation rather than sequence homology. This complexation with histones, as well as histone-deoxyribooligonucleotide complexes, suggests a site-specific nature, being influenced by the primary structures of peptides and oligonucleotides involved. Testagen appears to be interacting with histones, and may play a role in the conformation and functional state of chromatin, consequently influencing gene activity and cellular differentiation through epigenetic mechanisms. Understanding the exact pathways and impacts of these interactions would require further exploration and detailed studies into how such peptide-histone complexes influence gene transcription, DNA repair, replication, and other cellular processes influenced by chromatin structure.(5) Testagen and the Hypothalamic–Pituitary–Thyroid Axis In a thorough exploration of Testagen, its impact was conducted on hypophysectomized avian models. The models were apparently used to analyze the synthetic peptide's potential on the functional activity and morphological structure of the thyroid gland. Hypophysectomization, a procedure involving the removal or disabling of the pituitary gland, apparently induced a series of physiological alterations in the avian models, such as growth retardation, reduced excitability, and anorexia, along with changes including decreased body and thyroid gland weight, increased thyroid follicle size, and flattened thyrocytes. Furthermore, a notable decrease was reported in thyroid hormone concentrations, including thyroid-stimulating hormone (TSH), T3 (Triiodothyronine), T4 (Thyroxine), and free thyroxine.(3) After introducing Testagen there appeared to be distinct outcomes noticed among the avian models. An apparent 23% increase in body weight was suggested, complemented by a slight apparent augmentation in the thyroid gland's weight. Morphological adaptations also appeared to take place, such as an apparent reduction in the mean sectional area of follicles and a potential prevention of follicular epithelium flattening and colloid accumulation within the follicular cavity. Noteworthy appeared to be a well-defined interfollicular epithelium, coupled with variations in the nuclear-cytoplasmic ratio and a decrease in the height of thyrocytes, though these were considered less significant than in the control group. Additionally, Testagen exhibited an apparent stimulating impact on the growth of the thyroid capsule, despite the width of the thyroid capsule in these models still appearing to be inferior to that of control models.(3) Diving into the realm of aged avian models a normalization of the thyroid gland weight post-Testagen introduction was apparently observed. The synthetic peptide appeared to exert a moderate stimulating impact on the proliferation of epithelial cells. Consequently, the follicle size in these older avian models may have exceeded that of their younger counterparts. While the epithelium shape may have remained almost constant, a minor elevation was apparently seen in the nuclear-cytoplasmic ratio. Overall, the researchers suggested that the peptide may have better action in younger models and commented that “Restoration of the thyroid functions and morphology was registered to be greater in one-year-old chicken as compared to five-year-old ones.”(3) Testagen peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Fedoreyeva, L. I., Kireev, I. I., Khavinson, V. K.h, & Vanyushin, B. F. (2011). Penetration of short fluorescence-labeled peptides into the nucleus in HeLa cells and in vitro specific interaction of the peptides with deoxyribooligonucleotides and DNA. Biochemistry. Biokhimiia, 76(11), 1210–1219. https://doi.org/10.1134/S0006297911110022 Khavinson, V. K., Popovich, I. G., Linkova, N. S., Mironova, E. S., & Ilina, A. R. (2021). Peptide Regulation of Gene Expression: A Systematic Review. Molecules (Basel, Switzerland), 26(22), 7053. https://doi.org/10.3390/molecules26227053 Kuznik, B. I., Pateiuk, A. V., Rusaeva, N. S., Baranchugova, L. M., & Obydenko, V. I. (2011). Advances in gerontology = Uspekhi gerontologii, 24(1), 93–98. https://pubmed.ncbi.nlm.nih.gov/21809626/ Rossikhin, V. V., Hoshchenko, Y. O., & Osipov, P. G. (2011). EFFICACY OF TESTOSTERONE SYNTHESIS INDUCTOR APPLICATION" TESTAGEN" IN ANDROGENIC DEFICIENCY IN PATIENTS WITH CHRONIC ABACTERIAL PROSTATITIS. Problems of Endocrine Pathology, 36(2), 17-22. DOI: 10.21856/j-PEP.2011.2.03 Fedoreyeva, L. I., Smirnova, T. A., Kolomijtseva, G. Y., Khavinson, V. K., & Vanyushin, B. F. (2013). Interaction of short peptides with FITC-labeled wheat histones and their complexes with deoxyribooligonucleotides. Biochemistry (Moscow), 78, 166-175. https://doi.org/10.1134/S0006297913020053 { "@context": "https:\/\/schema.org", "@type": "Product", "name": "Testagen (20mg)", "description": "Testagen for sale online (20mg). Peptides for sale at 99% purity with top customer service. Get research study results and information.", "image": "https://www.painandanxietymeds.shop/wp-content/uploads/2023/10/Testagen-20mg-300x300.jpg", "offers": [ { "@type": "Offer", "priceCurrency": "USD", "price": "63", "availability": "https:\/\/schema.org\/InStock", "itemCondition": "https:\/\/schema.org\/NewCondition", "seller": { "@type": "Organization", "name": "painandanxietymeds.shop" }, "url": "https:\/\/www.painandanxietymeds.shop\/testagen-20mg/", "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": "2027-12-09T15:11:59+00:00" } ], "url": "https:\/\/www.painandanxietymeds.shop\/testagen-20mg/", "aggregateRating": { "@type": "AggregateRating", "ratingValue": 96, "bestRating": 100, "reviewCount": 118 }, "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.
Prostamax (20mg)
Prostamax, aka KEDP, is a synthetic tetrapeptide (Lys-Glu-Asp-Pro) classified among the Khavinson peptides, which researchers have suggested may exhibit primary repair potential on various tissues, notably in prostate cell cultures. It appears to influence the structural dynamics of chromatin, potentially activating previously repressed genes and altering chromosomal dynamics. This may include increasing in the frequency of sister chromatid exchanges and Ag-positive nucleolus organizer regions, indicating enhanced chromosomal exchange activities and changes in ribosomal RNA gene activity as well as reducing the frequency of large segments of C-pericentromeric heterochromatin, suggesting a decondensation action on the chromatin. In prostatic gland tissue cultures, Prostamax may have a role in stimulating reparation processes, reducing inflammation and preventing sclerotic and atrophic processes. Chemical Makeup Molecular formula: C20H33N5O9 Molecular weight: 487.5 g/mol Sequence: Lys-Glu-Asp-Pro Other known titles: KEDP, SCHEMBL6660498 Research and Clinical Studies The content presented here integrates recent findings from preliminary studies about Prostamax's potential, as evidenced by diverse experimental methods. Prostamax Peptide and Gene Expression Related to Cellular Aging One study highlights the potential impact of Prostamax on the chromatin structure in lymphocytes.(1) Chromatin, the complex of DNA and proteins found in cells, has been observed to undergo two stages of denaturation at specific temperatures and energy states, denoted as T(d)VII and T(d)VIII. Prostamax appears to induce notable changes in this chromatin structure. Specifically, it appears to cause a redistribution of heat among two endotherms, T(d)III and T(d)IV, and leads to a decrease in their temperatures by 2.9 and 1.0 degrees Celsius, respectively. This redistribution and temperature shift might be linked to a relaxation in the chromatin structure, particularly the 30-nm-thick fiber relaxing into a 10-nm filament. Furthermore, there's a suggestion that Prostamax may lead to minor structural alterations in the nucleosomal organization within the chromatin, indicated by a slight decrease in the temperatures of T(d)VIII and T(d)VII in lymphocytes introduced to Prostamax compared to control cells. These changes are possibly due to adjustments in the structural organization of both the 10-nm filament and the 30-nm fiber. Another trial further investigates the impact of Prostamax on several chromosomal characteristics in aged cells, revealing that Prostamax possibly influences these characteristics.(2) More specifically, the study suggests that Prostamax might have a modifying action on chromatin, particularly in the context of aging cells. This could potentially lead to the activation of previously repressed genes and changes in chromosomal dynamics. For example, Prostamax apparently increases the frequency of sister chromatid exchanges (SCE). In cells introduced to Prostamax, the frequency of SCE rose to an average of 12.0 exchanges per cell, compared to 5.9 exchanges in control cells. This suggests that Prostamax may have a role in enhancing chromosomal exchange activities. Furthermore, the study posits that Prostamax may potentially increase the frequency of Ag-positive nucleolus organizer regions (NORs). In Prostamax-exposed cells, the average was 2.5 Ag-positive NORs per cell, compared to just 0.95 in intact cells. This increase might indicate changes in ribosomal RNA gene activity or chromatin structure modifications. Prostamax also seemingly reduces the frequency of large segments of C-pericentromeric heterochromatin, particularly in chromosomes 1 and 9. This change might imply a decondensation and deheterochromatinization action on the chromatin, possibly leading to the release of genes previously repressed by heterochromatinization. Ultimately, the authors concluded that “basis for the protective action of Prostamax is its modifying effect on chromatin.” Another trial also reports that Prostamax may exhibit a potential to affect genetic processes in aging cells by modulating chromatin structure and possibly reactivating certain genes.(3) The trial focused on the potential role of Prostamax in the activation of ribosome genes, decondensation of chromatin, and altering the structure of heterochromatin. Prostamax, along with other peptides like Epitalon and Livagen, possibly led to the decondensation of chromosome 1 pericentromeric structural chromatin. This suggests that Prostamax may have a role in modulating the structure of chromatin in aging cells. The decondensation of chromatin is significant as it potentially indicates an activation of previously inactivated genes due to age-related chromatin condensation. The research posited that the peptides, including Prostamax, potentially "release" genes repressed as a result of the age-specific condensation of cellular euchromatin regions, referred to as deheterochromatinization of facultative chromatin. This implies that Prostamax may contribute to the reactivation of certain genetic activities that diminish with age. Furthermore, Prostamax possibly induced changes specifically in chromosome 1, suggesting a selective action on certain chromosomal regions. However, the exact mechanisms through which Prostamax exerts these actions, and the full scope of its potential impact on aging and age-related genetic processes, remain somewhat unclear and require further investigation. Prostamax Peptide and the Prostate Gland Prostamax has been the subject of research exploring its potential action on prostatic gland tissue cultures. One investigation, utilizing organotypic tissue cultures, incorporated explants from both young and aged murine models as the basis for the study.(4) The focus was to observe any possible stimulating action of Prostamax on these tissues. In the course of this research, Prostamax was introduced at a specific concentration, which was posited to potentially elicit a stimulating action on the prostatic gland tissue cultures. This action was observed when these cultures were compared to control explants, suggesting that Prostamax might have a role in stimulating reparative processes in prostatic tissues, especially during the aging process in these murine models. The authors suggested that peptide such as Prostamax may have potential “for the stimulation of reparative processes in the appropriate tissues while aging.” Another study explored the potential of Prostamax in models of chronic aseptic prostatitis.(5) Prostamax, through experimental studies, apparently indicated a capacity to reduce the intensity of chronic inflammation, such as swelling, hyperemia of vessels, and lymphoid infiltration in murine models. The experimental setup involved murine models that underwent a procedure designed to induce chronic aseptic inflammation in the prostate gland. Post-procedure, the models were exposed to Prostamax and its impact was then evaluated in contrast to active controls. The primary goal was to gauge the potential of Prostamax in lessening the impact of chronic prostatitis and its associated complications, and to compare its potential to active controls. The authors of this study suggested that Prostamax might have the capability to diminish inflammation-related symptoms such as swelling, vessel hyperemia, and cellular infiltration commonly seen in murine models of chronic prostatitis. Notably, it also seemed to have a role in possibly curtailing the development of sclerotic and atrophic processes in the prostate gland models. These processes are typically seen as complications in such models and their potential mitigation by Prostamax is a point of interest. Prostamax's potential in preventing these processes appeared more pronounced compared to the comparator agents, suggesting its superiority in this regard. Additionally, Prostamax was observed to possibly enhance sexual activity in the animal models, a finding that may indicate broader research potential. Prostamax peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Meskhi T, Khachidze D, Barbakadze Sh, Madzhagaladze G, Gorgoshidze M, Monaselidze D, Lezhava T, Tadumadze N. Vliianie peptidnogo bioreguliatora prostamaksa na geterokhromatin limfotsitov cheloveka in situ [The influence of the peptide bioregulator prostamax on heterochromatin of human lymphocytes in situ]. Biofizika. 2004 Nov-Dec;49(6):1091-3. Russian. PMID: 15612551. Dzhokhadze TA, Buadze TZh, Gaĭozishvili MN, Baratashvili NA, Lezhava TA. [Deheterochromatinization of the chromatin in old age induced by oligopeptide bioregulator (Lys-Glu-Asp-Pro)]. Georgian Med News. 2012 Nov;(212):76-82. Russian. PMID: 23221144. Khavinson VKh, Lezhava TA, Malinin VV. Effects of short peptides on lymphocyte chromatin in senile subjects. Bull Exp Biol Med. 2004 Jan;137(1):78-81. doi: 10.1023/b:bebm.0000024393.40560.05. PMID: 15085253. Zakutskiĭ AN, Chalisova NI, Ryzhak GA, Aniskina AI, Filippov SV, Zeziulin PN. [The tissue-specific effect of synthetic peptides-biologic regulators in organotypic tissues culture in young and old rats]. Adv Gerontol. 2006;19:93-6. Russian. PMID: 17152728. Borovskaya, T. G., Pakhomova, A. V., Vychuzhanina, A. V., Poluektova, M. E., Fomina, T. I., Ermolaeva, L. A., ... & Neplochov, E. A. (2013). Experimental studying of the drug efficiency Prostamax in the therapy of chronic aseptic prostatitis and its complications. Modern Research in Inflammation, 2013. 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.
TB-500 (Thymosin Beta 4) (5mg / 10mg)
TB-500 peptide, also known as synthetic Thymosin Beta 4 or Tβ4 is the synthetic version of the naturally occurring protein Thymosin beta 4. The latter is found naturally within the cells of the thymus organ and encoded by the TMSB4X gene. Researchers have suggested TB-500 peptide hosts similar potential as Thymosin beta 4. These potential mechanisms of action may include inducing angiogenesis, elevating wound healing, or possibly elevated metastatic potential of tumor cells and hair growth. Besides being highly soluble in water and light in weight, TB-500 is a 43 amino acid-containing peptide found in abundance in the wound fluid comprising multiple blood platelets. This peptide may exhibit possible anti-inflammatory potential and may support neurological healing, as well as potentially supporting healing processes in the spinal cord, heart, and epidermis.(1) Overview TB-500 peptide, also known as thymosin β(4), includes a distinct peptide segment (17)LKKTETQ(23), which acts as the active site and which researchers consider potentially impactful in actin binding, cell migration, and wound healing.(2) The amino acid sequence of TB-500 is: Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH. Actins are essential proteins that form a key component of the cytoskeleton within cells, serving not only to maintain cellular structure but also to facilitate various cellular functions, including movement. Actin is suggested to be critical in supporting these cellular structures and processes. Thymosin beta-4 and, thus, TB-500 are believed to interact with actin, potentially by binding to globular actin (G-actin), a precursor to filamentous actin (F-actin). This interaction is thought to hinder the transformation of G-actin into F-actin, a process known as actin sequestration, and is likely to increase the availability of G-actin. The inhibition of F-actin formation by thymosin beta-4 may conceivably modify the structure of the cellular cytoskeleton, impacting cellular abilities for movement and morphological changes. Such changes are tentatively linked to various physiological and pathological states where cell motility is essential, including wound healing, tissue regeneration, and the progression of cancer through metastasis.(3) Furthermore, Thymosin beta-4 has been detected not only within cells but also extracellularly, such as in blood plasma and wound exudates. Preliminary studies involving vascular cells suggest that Thymosin beta-4 is extracellular, it might influence cellular functions like motility and the formation of new blood vessels (angiogenesis).(11,12) It is postulated that Thymosin beta-4 might exert this potential through its interactions with ATP synthase enzymes located on the cell surface, which are critical for cellular energy production. These findings indicate a broader scope of action for thymosin beta-4, impacting both intra- and extracellular processes. Chemical Makeup Molecular Formula: C212H350N56O78S Molecular Weight: 4963 g/mol Other Known Titles: Thymosin Beta 4 Research and Clinical Studies TB-500 Peptide and Inflammation Tβ4, and thus TB-500, is thought to potentially increase the levels of microRNA-146a (miR-146a), which might function as a suppressive regulator of specific cellular signaling pathways, particularly those associated with the functions of inflammation-related cytokines, including L-1 receptor-linked kinase 1 (IRAK1) and tumor necrosis factor receptor-associated factor 6 (TRAF6). The researchers of a study investigating the potential of the peptide on these factors propose this as a possible mechanism of action for TB-500. More specifically, the authors observed that "transfection of anti-miR-146a nucleotides reversed the inhibitory effect of Tβ4 on IRAK1 and TRAF6," thus suggesting this as a potential mechanism. Consequently, it is suggested that TB-500 may contribute to anti-inflammatory potential via these mechanisms.(4) TB-500 Peptide and Acute Wounds In 1999, a research study was conducted on wounded murine test models, who were introduced to TB-500 as a form of synthetic Thymosin Beta 4.(5) Four days after the presentation, it was reported by the researchers that the TB-500 peptide rats exhibited an apparent 41% increase in re-epithelialization than control murine models presented with saline. Seven days after the study, the TB-500 wounds were reported to be contracted by at least 11% more than the saline wounds. Upon analysis, it was concluded that TB-500 may possibly induce angiogenesis and collagen deposition, increasing the wound healing rate.The authors commented that their observations “suggest that Tβ4 is a potent wound healing factor with multiple activities...” TB-500 Peptide and Chronic Wounds Research studies were carried out on normal rats and mice, diabetic mice, aged mice, and steroid-influenced rats. All these animals were served full-thickness punch wounds and introduced to the TB-500 peptide. It was reported that the TB-500 appeared to accelerate the wound-healing process in all test models, regardless of the stated pre-existing conditions. Furthermore, phase 2 clinical trials were conducted on models of stasis and pressure ulcers. It was reported that TB-500 might accelerate the healing process by as much as one month.(6) TB-500 Peptide and Heart Cells Pulmonary hypertension is considered by scientists to be a progressive cardiac disease where the pulmonary arteries restrict the blood ejection by the right ventricle. This may result in increased pulmonary vascular resistance and pressure, potentially leading to ventricular failure of the heart. It was reported by researchers that TB-500 might be action specific on the Notch3-Col 3A-CTGF gene axis in MCT-influenced mice, which appeared to result in the case of the test study in decreasing the right ventricular heart cell hypertrophy by a significant amount.(7) Based on Tβ4 research, TB-500 might also influence the regeneration of cardiac cells. Preliminary research indicates that TB-500 may enhance the resilience of myocardial cells under hypoxic conditions and may also promote angiogenesis, which could facilitate the repair of cardiac cells. There is a suggestion from researchers that cardiac fibroblasts could potentially differentiate into cells akin to cardiomyocytes.(8) Furthermore, it has been proposed that the combination of TB-500 with cardiac reprogramming methods could synergistically mitigate damage to cardiac cells and support their regeneration by activating intrinsic cells in the heart area. Further experimentation employing mouse models, in which coronary arteries were ligated, suggested that TB-500 could potentially increase the activity of integrin-linked kinase (ILK) and protein kinase B (Akt) in cardiac tissue. This observation indicates a possible enhancement in the early survival of cardiomyocytes and an apparent improvement in cardiac function.(9) Further, the research indicates that TB-500 may facilitate the migration of myocardial and endothelial cells in the fetal heart, and this function appears to be preserved in adult cardiomyocytes. TB-500 and Hair Follicle Growth In 2003, studies were carried out on mice to examine the potential of TB-500 in hair growth. Under the influence of the TB-500 peptide, it was reported by the researchers that, via histological examination of the mouse skin cells, the peptide appeared to increase the number of hair shafts and hair follicles, thereby inducing hair growth. Upon real-time PCR and western blotting techniques, changes in the expression of m-RNA cells were observed between the TB500 and control mice. The m-RNA and protein levels were reported elevated in TB-500 mice, which might have significantly induced hair growth.(10) TB-500 and Blood Vessel Formation It is hypothesized that TB-500 might influence angiogenesis via several molecular interactions. This is based on studies involving TB-500 overexpression lentiviral vector in transfecting umbilical vein endothelial cells (HUVEC) and murine critical limb ischemia (CLI) models.(13) Researchers have also employed inhibitors such as DAPT, targeting the Notch pathway, and BMS, affecting the NF-κB pathway, in both HUVEC and murine CLI experiments to probe the intricate biological processes involved. The potential of TB-500 on angiogenesis and cellular migration were evaluated using MTT assays to measure cell viability, alongside tube formation and wound healing assays to assess angiogenic and migratory capabilities, respectively. Additionally, a variety of molecular methodologies were utilized, including Western blotting, reverse transcription, quantitative PCR, immunofluorescence, and immunohistochemistry. These techniques were instrumental in investigating the expression levels of angiogenesis-associated markers and elements related to the Notch/NF-κB pathways. Preliminary findings indicate that TB-500 might enhance not only the viability, angiogenesis, and migration of HUVEC but could also elevate the expression of angiopoietin-2 (Ang2), TEK receptor tyrosine kinase 2 (tie2), vascular endothelial growth factor A (VEGFA), NOTCH1 intracellular domain (N1ICD), Notch receptor 3 (Notch3), NF-κB, and phosphorylated (p)-p65 in these cells. In the muscle tissues of murine CLI models, similar increases in the expression of CD31, α-smooth muscle actin (α-SMA), Ang2, tie2, VEGFA, N1ICD, and p-p65 were observed, suggesting a regulatory potential of TB-500 on these molecular targets. Interestingly, the application of DAPT and BMS in these studies seemed to counteract the actions of TB-500, potentially indicating that the mechanisms of action of TB-500 in promoting angiogenesis might be mediated through its interactions with the Notch and NF-κB pathways. Moreover, the apparent reversal of the actions of DAPT and BMS by TB-500 could underscore its role in modulating these pathways, supporting the proposition of its regulatory functions in angiogenesis. Researchers have noted that these observations might imply a role for Tβ4 in promoting angiogenesis through regulation of these critical pathways. TB-500 and Corneal Tissues Studies have posited that TB-500 may modulate cytokine production and thus accelerate healing in corneal wound models.(14) Following injury, there is some indication that TB-500 could promote increased expression of IL-1β and IL-6 mRNA in the corneas of murine models. Moreover, TB-500 experimentation after alkali injury might lead to a decrease in the expression of chemoattractants such as MIP-2 and KC for polymorphonuclear neutrophils (PMNs) in mouse corneas, potentially resulting in diminished PMN infiltration. Concerning the inflammatory signaling pathways in the cornea, it is speculated that TB-500 may influence NFκB pathways, possibly exerting anti-inflammatory actions. TB-500 is also theorized to possess anti-apoptotic attributes. An overexpression of TB-500 in cellular models is observed to potentially increase growth rates, diminish basal apoptosis, and confer resistance to factors that induce cell death. In corneal epithelial cells, TB-500 could potentially inhibit apoptosis by blocking caspases and curtailing the release of the pro-apoptotic protein bcl-2 from mitochondria. The mechanism of TB-500’s anti-apoptotic action might include reducing the initiation signals of early cell death and activating the survival kinase Akt via complex interactions with PINCH and integrin-linked kinase. It is conceivable that TB-500’s anti-apoptotic influence operates through several molecular pathways. Nonetheless, it is crucial to acknowledge that these mechanisms remain conjectural and warrant further empirical investigation to be substantiated. TB-500 peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Kleinman HK, Sosne G. Thymosin β4 Promotes Dermal Healing. Vitam Horm. 2016;102:251-75. doi: 10.1016/bs.vh.2016.04.005. Epub 2016 May 24. Ho EN, Kwok WH, Lau MY, Wong AS, Wan TS, Lam KK, Schiff PJ, Stewart BD. Doping control analysis of TB-500, a synthetic version of an active region of thymosin β₄, in equine urine and plasma by liquid chromatography-mass spectrometry. J Chromatogr A. 2012 Nov 23;1265:57-69. doi: 10.1016/j.chroma.2012.09.043. Epub 2012 Sep 23. Gurtner GC, Werner S, Barrandon Y, Longaker MT. Wound repair and regeneration. Nature. 2008 May 15;453(7193):314-21. doi: 10.1038/nature07039. PMID: 18480812. Santra, M., Zhang, Z. G., Yang, J., Santra, S., Santra, S., Chopp, M., & Morris, D. C. (2014). Thymosin β4 up-regulation of microRNA-146a promotes oligodendrocyte differentiation and suppression of the Toll-like proinflammatory pathway. The Journal of biological chemistry, 289(28), 19508–19518. https://doi.org/10.1074/jbc.M113.529966 Katherine M. Malinda et.al, Thymosin β4 Accelerates Wound Healing, Journal of Investigative Dermatology, Volume 113, Issue 3, 1999, Pages 364-368, ISSN 0022-202X. Treadwell T, Kleinman HK, Crockford D, Hardy MA, Guarnera GT, Goldstein AL. The regenerative peptide thymosin β4 accelerates the rate of dermal healing in preclinical animal models and in patients. Ann N Y Acad Sci. 2012 Oct. Wei C, Kim IK, Li L, Wu L, Gupta S. Thymosin Beta 4 protects mice from monocrotaline-induced pulmonary hypertension and right ventricular hypertrophy. PLoS One. 2014 Nov 20;9(11):e110598. Srivastava, D., Ieda, M., Fu, J., & Qian, L. (2012). Cardiac repair with thymosin β4 and cardiac reprogramming factors. Annals of the New York Academy of Sciences, 1270, 66–72. https://doi.org/10.1111/j.1749-6632.2012.06696.x Bock-Marquette, I., Saxena, A., White, M. D., Dimaio, J. M., & Srivastava, D. (2004). Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair. Nature, 432(7016), 466–472. https://doi.org/10.1038/nature03000 Gao, Xy., Hou, F., Zhang, Zp. et al. Role of thymosin beta 4 in hair growth. Mol Genet Genomics 291, 1639–1646 (2016). Huff, T., Müller, C. S., Otto, A. M., Netzker, R., & Hannappel, E. (2001). beta-Thymosins, small acidic peptides with multiple functions. The international journal of biochemistry & cell biology, 33(3), 205–220. https://doi.org/10.1016/s1357-2725(00)00087-x Freeman, K. W., Bowman, B. R., & Zetter, B. R. (2011). Regenerative protein thymosin beta-4 is a novel regulator of purinergic signaling. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 25(3), 907–915. https://doi.org/10.1096/fj.10-169417 Lv, S., Cai, H., Xu, Y., Dai, J., Rong, X., & Zheng, L. (2020). Thymosin‑β 4 induces angiogenesis in critical limb ischemia mice via regulating Notch/NF‑κB pathway. International journal of molecular medicine, 46(4), 1347–1358. https://doi.org/10.3892/ijmm.2020.4701 Sosne, G., Qiu, P., & Kurpakus-Wheater, M. (2007). Thymosin beta 4: A novel corneal wound healing and anti-inflammatory agent. Clinical ophthalmology (Auckland, N.Z.), 1(3), 201–207. 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.
Pinealon (20mg)
Pinealon is a short synthetic peptide composed of three amino acids Glu-Asp-Arg, also known as the EDR peptide.(1)(2) Pinealon is suggested to impact the central nervous system, which may lead to behavior modification while also possibly protecting neurons and various cell types from oxidative stress. The primary research focus on this peptide is evaluating its potential to penetrate the blood-brain barrier, cellular membrane, and nuclear membrane. However, researchers have also suggested that it may also interact directly with DNA molecules. Pinealon tripeptide is isolated from another chemical compound, Cortexin.(2) Cortexin is a polypeptide with a particularly low molecular weight. Due to this low weigh, Cortexin has been suggested by researchers to cross the blood-brain barrier to produce potential stimulatory action on the neurotransmitters in the brain.(3) Overview The neuroprotective and anti-apoptotic potential of the Pinealon peptide has been posited by researchers to be exerted via the MAPK / ERK signaling pathway.(2) The ERK signaling cascade may play a role in the phosphorylation of the substrates, which may lead to elevated neuron plasticity and increased cellular stress. In turn, this action may lead to cellular apoptosis. Similarly, MAPK signaling has been associated with certain metabolic disorders and inflammatory reactions. Researchers suggest that Pinealon may potentially reduce the synthesis of reaction oxygen species (ROS) on the cellular level. ROS is considered a messenger to MAPK and ERK signaling pathways, and the reduced synthesis may lead to a reduction in signaling reactions, preventing cellular stress and cell death.(2) Studies on Pinealon have suggested a concentration-dependent action. At lower concentrations, the peptide may potentially restrict the synthesis and subsequent accumulation of ROS and cell death. In comparison, the peptide might lead to a modulation of the cell cycle at higher concentrations. Researchers reporting this apparent correlation in peptide presence have suggested that it may exert antioxidant potential at lower concentrations while possibly interacting with the cell genome and altering the cell cycle.(4) Chemical Makeup Molecular Formula: C15H26N6O8 Molecular Weight: 418.4 g/mol Other Known Titles: EDR, Glu-Asp-Arg Research and Clinical Studies Pinealon Peptide and Cell Aging The main purpose of this clinical study was to analyze the cellular and metabolic aspects of synthetic tripeptides, including Pinealon and a similar peptide called Vesugen. As part of this study,(5) research models of poly-morbidity and organic brain syndrome were observed. Both peptides exhibited apparent anabolic potential; researchers reported improvement in the functioning of the central nervous system and other vital organs compared to control models. The peptides did not appear to affect the degree of chromatin condensation, which the researchers indicated may suggest that the peptides do not act on cellular levels. Another separate study(6) has suggested that the Pinealon peptide may potentially act on muscle cells, modulating the levels of irisin. Scientists consider irisin to be central to muscle cell protection and mainly secreted during physical strain. Irisin may lead to the burning of excessive fat cell stores and is assumed by researchers to induce an elongation of telomeres (DNA caps) as well. By potentially increasing irisin levels, Pinealon may potentially exert protection of DNA telomeres and counteract cell aging action to some degree. Pinealon Peptide and Prenatal Hyperhomocysteinemia Scientists characterize hyperhomocysteinemia by the excessive concentration of homocysteine (HC) amino acid in the blood, indicating extreme vitamin deficiency, which might lead to an increased risk of neurological deterioration.(7) The main goal of this study(8) was to determine the potential of Pinealon on experimentally induced hyperhomocysteinemic pregnant female murine models. The female rats were given methionine from their second trimester onwards, which appeared to lead to increased concentration of homocysteine (HC) levels. The rat offspring from the control and the experimental models were then observed for this study. Upon analysis, it was suggested by the researchers that the peptide did not appear to reduce or inhibit the development of homocysteine in the offspring, however, there appeared to be some action seen in the experimental models, as they appeared to exhibit increased cognitive processing. The researchers suggested that the peptide did not appear to induce the metabolism of homocysteine but may have led to reduced toxic action of the compound. Pinealon Peptide and Serotonin Expression Studies(9) were conducted on the isolated brain cell cultures where the Pinealon peptide was presented. Upon analysis, it was suggested that the peptide might stimulate levels of serotonin expression in the cell cultures. Preliminary results seemed to indicate that after exposure to Pinealon, there was a notable increase in serotonin synthesis compared to the control groups. This increase was quantitatively assessed to be 1.9 times greater in younger cell cultures. The molecular dynamics behind this observed action might involve Pinealon's interaction with the DNA. It is speculated that this augmentation in serotonin production may be facilitated by Pinealon's potential to bind specifically to a DNA sequence within the promoter region of the gene encoding 5-tryptophan hydroxylase, an enzyme considered to be critical for serotonin synthesis. More specifically, the peptide is hypothesized to bind to a particular nucleotide sequence in the promoter region of the 5-tryptophan hydroxylase gene, potentially enhancing the transcriptional activity of the gene and thus increasing 5-tryptophan hydroxylase enzyme production. Additionally, molecular docking simulations were employed to formulate hypotheses about the peptide’s binding orientation and stability with the DNA. These simulations, which consider factors like hydrophobic interactions, electrostatic forces, and hydrogen bonding, indicated a lower (negative) binding energy for Pinealon compared to another peptide, Lys-Glu-Asp. Such a decrease in binding energy suggests a more stable potential interaction with DNA, which might lead to elevated levels of 5-tryptophan hydroxylase enzyme synthesis and, subsequently, increased serotonin production. Scientists consider serotonin a key mood-stabilizing hormone, and further studies are being conducted to observe the potential of Pinealon on serotonin synthesis. Another study suggests that Pinealon may potentially influence serotonin levels in the cerebral cortex of murine models under conditions of mild hypothermia. The possible elevation of serotonin levels postulated in the research might indicate that Pinealon could be involved in modulating these aspects of brain function, particularly in response to stress induced by mild hypothermia.(10) The same study also suggests that such models may exert an accumulation of adrenergic mediators when exposed to Pinealon and acute hypobaric hypoxia. Adrenergic mediators are chemicals that transmit nerve impulses and may potentially influence various brain functions, particularly under stress. The increase in these mediators might indicate a response mechanism of Pinealon that may be associated with neuroprotective activities. Pinealon Peptide and Anti-apoptotic Potential Studies(11) have suggested that Pinealon peptide may impact the levels of the caspase 3 enzyme. Scientists consider the caspase 3 enzyme an initiator of cell apoptosis (controlled cell death). When Pinealon peptide was presented in experimental murine models of ischemic stroke, the peptide appeared to modulate the levels of this enzyme, thereby shutting down the pathway of cellular death. This, in turn, reportedly reduced hypoxia action during the stroke. The research posits that Pinealon may play a role in reducing neuroinflammation and potentially restoring neurogenic processes to their reference levels, presumably those observed under normoxic (normal oxygen) conditions. By potentially fostering an environment conducive to neurogenesis during hypoxic stress, researchers also posit that Pinealon may contribute to the brain's resilience against oxygen deprivation. In addition to its apparent role in modulating the activity of caspase-3, Pinealon was also suggested to influence levels of interleukin-6 and tumor necrosis factor. Interleukin-6 and tumor necrosis factors are cytokines commonly linked with inflammation and cellular stress responses. The implication is that Pinealon might help bring these inflammatory markers back to baseline levels, thus potentially mitigating the inflammatory response and apoptosis triggered by hypoxic conditions. The action of suppressing the caspase 3 enzyme was also observed in skin cells. By reducing cellular apoptosis, the peptide may potentially stimulate cell proliferation, possibly leading to an increased regenerative process.(12) Pinealon peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Khavinson, V., Linkova, N., Kozhevnikova, E., & Trofimova, S. (2020). EDR Peptide: Possible Mechanism of Gene Expression and Protein Synthesis Regulation Involved in the Pathogenesis of Alzheimer's Disease. Molecules (Basel, Switzerland), 26(1), 159. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7795577/ National Center for Biotechnology Information. PubChem Compound Summary for CID 10273502, Glu-Asp-Arg. https://pubchem.ncbi.nlm.nih.gov/compound/Glu-Asp-Arg Eroğlu, O., Karlıdağ, T., Kuloğlu, T., Keleş, E., Kaygusuz, İ., & Yalçın, Ş. (2018). The Protective Effect of Cortexin on Cisplatin-Induced Ototoxicity. The journal of international advanced otology, 14(1), 27–33. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6354512/ Khavinson V, Ribakova Y, Kulebiakin K, Vladychenskaya E, Kozina L, Arutjunyan A, Boldyrev A. Pinealon increases cell viability by suppression of free radical levels and activating proliferative processes. Rejuvenation Res. 2011 Oct;14(5):535-41. https://pubmed.ncbi.nlm.nih.gov/21978084/ 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. https://pubmed.ncbi.nlm.nih.gov/26390612/ Khavinson VKh, Kuznik BI, Tarnovskaya SI, Lin'kova NS. Short Peptides and Telomere Length Regulator Hormone Irisin. Bull Exp Biol Med. 2016 Jan;160(3):347-9. doi: 10.1007/s10517-016-3167-y. Epub 2016 Jan 8. PMID: 26742748. https://pubmed.ncbi.nlm.nih.gov/26742748/ Homocysteine. https://my.clevelandclinic.org/health/articles/21527-homocysteine Arutjunyan, A., Kozina, L., Stvolinskiy, S., Bulygina, Y., Mashkina, A., & Khavinson, V. (2012). Pinealon protects the rat offspring from prenatal hyperhomocysteinemia. International journal of clinical and experimental medicine, 5(2), 179–185. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3342713/ Khavinson, V.K., Lin’kova, N.S., Tarnovskaya, S.I. et al. Short Peptides Stimulate Serotonin Expression in Cells of Brain Cortex. Bull Exp Biol Med 157, 77–80 (2014). https://link.springer.com/article/10.1007/s10517-014-2496-y#citeas Mendzheritsky AM, Karantysh GV, Ryzhak GA, Prokofiev VN. [Pinealon and Cortexin influence on behavior and neurochemical processes in 18-month aged rats within hypoxia and hypothermia]. Adv Gerontol. 2015;28(3):532-539. Russian. PMID: 28509493. Mendzheritskiĭ AM, Karantysh GV, Ryzhak GA, Dem'ianenko SV. [Regulation of content of cytokines in blood serum and of caspase-3 activity in brains of old rats in model of sharp hypoxic hypoxia with Cortexin and Pinealon]. Adv Gerontol. 2014;27(1):94-7. Russian. PMID: 25051764. https://pubmed.ncbi.nlm.nih.gov/25051764/ Voicekhovskaya MA, Chalisova NI, Kontsevaya EA, Ryzhak GA. Effect of bioregulatory tripeptides on the culture of skin cells from young and old rats. Bull Exp Biol Med. 2012 Jan;152(3):357-9. doi: 10.1007/s10517-012-1527-9. PMID: 22803085. https://pubmed.ncbi.nlm.nih.gov/22803085/ 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.