Medicines & Treatments
Syn-Coll (Palmitoyl Tripeptide-5) (200mg)
Syn-Coll is a synthetic peptide compound, also known as palmitoyl tripeptide-5. It was designed to mimic the activity of thrombospondin-1 (TSP-1), a natural extracellular matrix protein that apparently stimulates transforming growth factor beta (TGF-β). TGF-β is a crucial growth factor that plays a vital role in maintaining skin integrity and stimulating the postnatal development of skin structures by promoting collagen synthesis. The short sequence Lys-Arg-Phe-Lys of TSP-1 is considered responsible for TGF-β stimulation.(1) Syn-Coll has the sequence of Palmitoyl-Lys-Val-Lys, and scientists report that it may exert similar action on TGF-β. As a result, animal models and dermal fibroblasts cell culture tests suggest it may stimulate collagen production. More specifically, Syn-Coll may increase the production of Type I and Type III collagen by dermal fibroblasts via stimulating TGF-β activity. Furthermore, Syn-Coll has been extensively studied in animal models and experiments, which all generally hypothesize that it exhibits some potential to increase collagen synthesis but also prevent collagen degradation. Syn-Coll may prevent collagen breakdown by inhibiting the activity of matrix metalloproteinases (MMPs) such as MMP1 and MMP3. Chemical Makeup Molecular Formula: C33H65N5O5 Molecular Weight: 611.9 g/mol Other Known Titles: Palmitoyl-lysyl-valyl-lysine, Palmitoyl Tripeptide-5 Research and Clinical Studies Syn-Coll Peptide and Collagen Synthesis Collagen is a major component of the extracellular matrix, the network of proteins and fibers that comprise dermal connective tissue. Recent studies have indicated that Syn-Coll may stimulate collagen synthesis. This synthetic peptide is believed to work by mimicking the activity of TSP-1 to activate the growth factor TGF-β. More specifically, Syn-Coll may work by mimicking part of the sequence of TSP-1.(2) TGF-β is a crucial growth factor that has been suggested to play an important role in regulating collagen production. Studies have suggested that Syn-Coll works by activating latent TGF-β, thereby increasing the production of type I and type III collagen by dermal fibroblasts. As a result, scientists report that activating TGF-β "causes a persistent increase in steady-state amounts of type I and type III collagen and fibronectin mRNAs in normal [...] dermal fibroblasts."(3) Trials have also indicated that Syn-Coll may increase type 1 collagen synthesis via TGF-β to a greater degree than other peptides, such as palmitoyl pentapeptide.(4) The researchers posited that "Palmitoyl tripeptide-5 also known as Syn-Coll, increases collagen 1 production via TGF-b reportedly 60% more effective than palmitoyl pentapeptide." Syn-Coll Peptide and Collagen Breakdown Matrix metalloproteinases (MMPs) are a group of enzymes involved in the degradation of extracellular matrix proteins, including collagen. Scientists consider MMPs to be typically produced by dermal cells, such as fibroblasts, and are involved in tissue remodeling and maintaining the extracellular matrix. However, they further posit when MMPs are overproduced or become dysregulated, they can contribute to dermal collagen breakdown. For example, MMP-1 is considered to be an enzyme that specifically degrades type I collagen. Fibroblasts produce MMP-1, and its activity may be increased by factors such as UV radiation, inflammation, and oxidative stress. Another member of the MMPs is MMP-3, and considered capable of cleaving a wide range of extracellular matrix proteins, including collagens, laminin, fibronectin, proteoglycans, and elastin. It may be particularly active at degrading type II collagen, the main structural component of cartilage. MMP-3 has also been implicated in the degradation of other collagens, such as type III collagen, which is abundant in the skin and blood vessels. Syn-Coll (Palmitoyl tripeptide-5) seems to decrease collagen breakdown by inhibiting matrix metalloproteinases degrading collagen. More specifically, studies suggest that Syn-Coll (palmitoyl tripeptide-5) may prevent collagen breakdown by interfering with MMP1 and MMP3 collagen degradation.(5) Syn-Coll Peptide and Anti-Aging Studies have suggested that Syn-Coll may reduce the appearance of wrinkles to a much greater extent than a placebo.(6) The scientists reported that "formulation demonstrated a dose-dependent wrinkle reduction, measured by PRIMOS surface topography." Ultimately, they concluded that Syn-Coll (palmitoyl tripeptide-5) might exhibit roughly 3.5 times the potential to reduce the appearance of wrinkles than the placebo. One study in 60 test subjects that lasted 84 days reported that Syn-Coll twice daily suggested it may exhibit anti-wrinkle potential and reduce skin roughness better than control groups, placebo, and other peptides.(7) The peptide appeared to reduce wrinkle parameters by 12%. Besides its potential on collagen synthesis and degradation, scientists suggest that Syn-Coll may exert possible anti-wrinkle action through other mechanisms.(8) These include supporting the skin's barrier function by possibly preventing water loss from the skin's surface. This can help to maintain optimal hydration levels in the skin. Furthermore, Syn-Coll may act as a humectant, which can help absorb and retain water in the skin. It may also increase skin surface lipids and act as an emollient, providing partial occlusion, lubrication, and moisturization to the skin. In addition, Syn-Coll may also be modified by adding an L-ascorbate moiety (AA) at the C-terminus (Pal-KVK-AA), which may have a depigmentation impact. Studies have suggested that this conjugation may inhibit melanin synthesis.(9) By blocking melanin production, this modified version of Syn-Coll may help reduce hyperpigmentation caused by photoaging, UV light, oxidative stress, and other factors. Syn-Coll peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: Murphy-Ullrich, J. E., & Poczatek, M. (2000). Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology. Cytokine & growth factor reviews, 11(1-2), 59–69. https://doi.org/10.1016/s1359-6101(99)00029-5 Trookman, N. S., Rizer, R. L., Ford, R., Ho, E., & Gotz, V. (2009). Immediate and Long-term Clinical Benefits of a Treatment for Facial Lines and Wrinkles. The Journal of clinical and aesthetic dermatology, 2(3), 38–43. Varga, J., Rosenbloom, J., & Jimenez, S. A. (1987). Transforming growth factor beta (TGF beta) causes a persistent increase in steady-state amounts of type I and type III collagen and fibronectin mRNAs in normal human dermal fibroblasts. The Biochemical journal, 247(3), 597–604. https://doi.org/10.1042/bj2470597 Bucay, V. W., & Day, D. (2013). Adjunctive skin care of the brow and periorbital region. Clinics in plastic surgery, 40(1), 225–236. https://doi.org/10.1016/j.cps.2012.09.003 Errante, F., Ledwoń, P., Latajka, R., Rovero, P., & Papini, A. M. (2020). Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Frontiers in chemistry, 8, 572923. https://doi.org/10.3389/fchem.2020.572923 Gorouhi, F., & Maibach, H. I. (2009). Role of peptides in preventing or treating aged skin. International journal of cosmetic science, 31(5), 327–345. https://doi.org/10.1111/j.1468-2494.2009.00490.x Schneider, A. L. (2010). Evaluation of the penetration and efficacy of anti-aging compounds (Doctoral dissertation, Monash University). Kim, H. M., An, H. S., Bae, J. S., Kim, J. Y., Choi, C. H., Kim, J. Y., Lim, J. H., Choi, J. H., Song, H., Moon, S. H., Park, Y. J., Chang, S. J., & Choi, S. Y. (2017). Effects of palmitoyl-KVK-L-ascorbic acid on skin wrinkles and pigmentation. Archives of dermatological research, 309(5), 397–402. https://doi.org/10.1007/s00403-017-1731-6 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.
Vilon (20mg)
Vilon is a dipeptide composed of amino acids lysine and glutamic acid. It also goes by the name 'Lysylglutamic Acid or Lysylglutamate.'(1) It is the shortest peptide suggested to possess potential action in the immune system, possibly mitigate cancer cell proliferation, and potentially induce anti-aging action within cells, possibly working on tissues within the liver, heart, and kidney. Vilon appears to exert its potential by possible interaction with the chromatin structure. Vilon peptide research has also led to the postulating of several research hypotheses, including that the peptide may act to unroll chromatin structures, that it may activate ribosomal genes stimulating the synthetic process, that it may release inactive genes, and that it may not decondense the chromatin situated on each side of the centromere of the chromosome. Through its potential action on the chromatin, Vilon may possibly alter DNA structure to reactivate the genes and cells that have gone 'silent.' Overview Considered a bioregulator peptide, researchers speculate that Vilon may potentially support functions within the immune system, including in immunocompromised animal models. Researchers suggest Vilon may activate the interleukin-2 protein in spleen cells, which is considered critical in maintaining immune function.(3) It may stimulate the organism to fight against microbial infection and foreign bodies and prevent harmful autoimmune responses. Vilon has been suggested to activate white blood and spleen cells and potentially naturally boost the organism to protect against autoimmune elements. A study was conducted in 2002 with three bioregulatory peptides to study their potential on interleukin-2 mRNA synthesis in spleen cells. According to this study, “The intensity of interleukin-2 mRNA synthesis in splenocytes depended on the type, concentration, and duration of [exposure] with the peptides. Vilon and Epithalon were most potent, while Cortagen produced a less pronounced effect on interleukin-2 mRNA synthesis.”(3) Furthermore, research suggests that Vilon peptides may possibly mitigate autoimmune action by interacting with the thymus gland. The thymus gland is considered responsible for the proliferation of T-helper cells, and with the help of the Vilon peptide, this proliferation may be further enhanced. As per N N Sevostianiva et al., the Vilon peptide is “considered as a bioactive substance possessing immunomodulator and antiallergic activity.” (4) The research indicates that there is a potential for Vilon to enhance the expression of the CD5 molecule in embryonic thymic cells. Specifically, the data revealed a tentative increase of 78% in the expression levels of CD5 in rat thymic cells and a 45% increase in embryonic thymic cells compared with the baseline levels in the control group. CD5 is a marker important in the development and maturation of T-cells in the thymus, an organ considered pivotal for the generation of immune cells. The study further hypothesizes that Vilon may influence the maturation process of thymic cells, potentially steering the development of T-cell precursors more toward becoming CD4+ T-helper cells. T-helper cells are deemed critical components of the adaptive immune system, aiding in the activation and direction of other immune cells. Chemical Makeup Molecular formula: C11H21N3O5 Molecular weight: 257.30g/mol Other known titles: Lysylglutamate, normophthal, Lysylglutamic acid Vilon Research and Clinical Studies Extended research has produced a wide variety of hypotheses speculating on the action of the Vilon peptide, some detailed below: Vilon Peptide and Cellular Lifespan Vilon may potentially extend the average lifespan of certain animal models under laboratory conditions through an extension and mitigation of cell death. As stated above, Vilon has been suggested to exhibit potential in enhancing the immune system, improving physical endurance and energy levels, thereby possibly increasing average lifespan of animal test models.(5) Vilon is advised to study earlier in the test model lifespan rather than later for clearest possible action. Researchers hypothesize when a bioregulator like Vilon is exposed in vivo in lab models, it may only reverse 'silent' cells, exerting no apparent action on cells killed via apoptosis. In another experiment, researchers explored the potential of Vilon on spleen organotypic tissue cultures derived from murine models of differing ages. The findings from this investigation suggest that Vilon potentially influences the development of the explants.(6) Further research investigated research models where the peptide was introduced into the cultural medium of tissue explants derived from murine models at varying stages of development: 3 days, 3 weeks, and 2 years old. It was posited that Vilon induces morphological stability in the tissues while potentially activating both regeneration and functional activity of the cells involved. Interestingly, the results suggest that the impact of Vilon appeared to be more pronounced in explants from older murine models. This observation leads to the hypothesis that Vilon may have potential relevance in geriatric research, focusing on the mechanisms of cell aging and regeneration. The possibility that Vilon preferentially supports older tissues might be indicative of its role in modulating age-related cellular mechanisms or promoting stability in more senescent cells.(7) Another study examined the actions of low amounts of ionizing radiation, which apparently leads to accelerated cell aging of the thymus and spleen in murine models. Vilon was tested for its potential to mitigate this accelerated cellular aging process. The researchers tentatively suggest that Vilon partially inhibited the pro-aging action induced by the radiation. This research posits that Vilon might be of interest in the field of geriatric research, potentially as an agent to manage or reduce the impacts of cell aging in critical immune organs post-radiation exposure. The study highlights Vilon’s potential role in preserving organ function in an irradiated environment, which may be crucial for developing strategies against radiation-induced degeneration in murine models.(8) Vilon Peptide and Carcinogenic Cells Several studies suggest that peptide exhibits the potential to prevent some spread of carcinogenic cells by preventing the formation of new tumors, and potentially inhibiting existing tumors' growth.(9) Another study examined the potential of Vilon on the development of urinary bladder carcinogenesis in murine models exposed to N-butyl-N-(4-hydroxybutyl)nitrosamine (BBNA).(10) The experiment included a control group and a Vilon-exposed group. Each group began with 50 rats, all of which received BBNA. The primary observation was that the incidence of urinary bladder cancer cells was lower in the Vilon-exposed group compared to the control group. Specifically, cancer cells developed in 56% of the Vilon-exposed murine models versus 75.5% of the controls. This data possibly indicates that Vilon may have a moderating action on cancer cell development when exposed to BBNA. Further, the study noted a reduction in both the prevalence and severity of preneoplastic and early neoplastic changes in the urinary bladder mucosa in the Vilon-exposed murine models. In terms of morphological changes, the study reported fewer hyperplastic changes and lower malignancy rates in the Vilon group. There was a noticeable delay in the malignization of epithelial tissues in the Vilon group, suggesting a potential role of Vilon in modulating the rate or extent of tumor malignancy. Additionally, the average number of tumors per animal was lower in the Vilon group (1.5 tumors per rat) compared to the control group (2.6 tumors per rat), and the tumor cells in the Vilon-exposed rats appeared to manifest with a less aggressive growth pattern. The reduction in tumor aggressiveness and prevalence might indicate that Vilon has the potential to modulate the carcinogenic actions of BBNA. The findings suggest that Vilon, potentially acting as an immunomodulator, might inhibit the early stages of carcinogenesis as well as tumor progression in experimental models. One study contradicts this potential property of Vilon. According to this study, when used with chemotherapeutic agents derived from platinum ions, this peptide–platinum combination may be more harmful than helpful.(11) Unfortunately, since this study only considers one specific type of chemotherapeutic action, the results reported by researchers may be inconclusive. Vilon Peptide and the Gastrointestinal Tract Vilon peptide may act on gastrointestinal functionality by possibly enhancing the working mechanisms of certain enzymes in the gastrointestinal tract. By doing so, the peptide exhibits potential resistance towards GI-specific ailments, and may reduce leaky bowels in animal models.(12) Acting on the small intestinal muscles, Vilon peptide may ameliorate glucose accumulation and glycine absorption.(13) Vilon Peptide and Gene Expression Upon presenting the Vilon peptide, researchers have suggested it exhibits potential to alter the gene expression of 36 genes in the heart. When presented with Epitalon, this number was reported as 144 genes. This suggests the peptide's possible action on genetic expression in the cardiac system, possibly impacting hemodynamic actions.(14) Vilon Peptide and Fibrinolysis Researchers suggested in one study that Vilon exhibits the potential to stimulate fibrinolysis and increase the concentration of natural anticoagulants in the organsim, namely antithrombin III and protein C. It was also suggested to reduce insulin levels and possibly regulate the metabolism of carbohydrates.(15) This suggests a possible interplay between Vilon's actions on coagulation and glucose regulation, although the mechanisms behind this interaction are not fully elucidated in the study. Furthermore, the study posits that Vilon may have a stabilizing impact on the immune system. This is inferred from changes in various immune cell types and immunoglobulins; notably, a reduction in T-helpers, T-dependent and non-T-dependent NK cells, and a normalization in the levels of active T-lymphocytes, B-lymphocytes, and IgA. Such findings suggest that Vilon may modulate both innate and adaptive immune responses, which may be crucial for overall immune homeostasis. Further, Vilon is suggested to increase the permeability of mesenteric microvessels in the vascular system. As per N. Gavrisheva et al., these results indicate that “the preparation produces a potent homeostatic effect in the early period of chronic renal failure.”(16) Vilon peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: National Center for Biotechnology Information (2022). PubChem Compound Summary for CID 7010502, Lysylglutamic acid. Retrieved November 21, 2022 from https://pubchem.ncbi.nlm.nih.gov/compound/Lysylglutamic-acid Lezhava T, Khavison V, Monaselidze J, Jokhadze T, Dvalishvili N, Bablishvili N, Barbakadze S. Bioregulator Vilon-induced reactivation of chromatin in cultured lymphocytes from old people. Biogerontology. 2004;5(2):73-9. https://pubmed.ncbi.nlm.nih.gov/15105581/ Kazakova TB, Barabanova SV, Khavinson VKh, Glushikhina MS, Parkhomenko EP, Malinin VV, Korneva EA. In vitro effect of short peptides on expression of interleukin-2 gene in splenocytes. Bull Exp Biol Med. 2002 Jun;133(6):614-6. https://pubmed.ncbi.nlm.nih.gov/12447482/ Sevostianova NN, Linkova NS, Polyakova VO, Chervyakova NA, Kostylev AV, Durnova AO, Kvetnoy IM, Abdulragimov RI, Khavinson VH. Immunomodulating effects of Vilon and its analogue in the culture of human and animal thymus cells. Bull Exp Biol Med. 2013 Feb;154(4):562-5. English, Russian. https://pubmed.ncbi.nlm.nih.gov/23486604/ Khavinson VK, Anisimov VN, Zavarzina NY, Zabezhinskii MA, Zimina OA, Popovich IG, Shtylik AV, Malinin VV, Morozov VG. Effect of vilon on biological age and lifespan in mice. Bull Exp Biol Med. 2000 Jul;130(7):687-90. DOI: 10.1007/BF02682106. PMID: 11140587. https://pubmed.ncbi.nlm.nih.gov/11140587/ Bykov NM, Chalisova NI. Osobennosti deĭstviia ul'tramalykh doz vilona v organotipicheskoĭ kul'ture selezenki krys raznogo vozrasta [Characteristics of effect of ultralow doses of vilon in organotypic culture of spleens from rats of various ages]. Adv Gerontol. 2002;10:85-7. Russian. PMID: 12577696. Kniaz'kin IV, Iuzhakov VV, Chalisova NI, Grigor'ev EI. Funktsional'naia morfologiia organotipicheskoĭ kul'tury selezenkoi krys razlichnogo vozrasta pri deĭstvii vilona [Functional morphology of organotypic culture of spleens from rats of various ages exposed to vilon]. Adv Gerontol. 2002;9:110-5. Russian. PMID: 12096432. Kniaz'kin IV, Poliakova VO. Deĭstvie vilona na timus i selezenku v radiatsionnoĭ modeli prezhdevremennogo stareniia [The effect of vilon on the thymus and spleen in a radiation model of premature aging]. Adv Gerontol. 2002;9:105-9. Russian. PMID: 12096431. Khavinson VKh, Anisimov VN. A synthetic dipeptide vilon (L-Lys-L-Glu) inhibits the growth of spontaneous tumors and increases the life span of mice. Dokl Biol Sci. 2000 May-Jun;372:261-3. PMID: 10944717. https://pubmed.ncbi.nlm.nih.gov/10944717/ Pliss GB, Mel'nikov AS, Malinin VV, Khavinson VK. Inhibitory effect of peptide vilon on the development of induced rat urinary bladder tumors in rats. Bull Exp Biol Med. 2001 Jun;131(6):558-60. doi: 10.1023/a:1012354603132. PMID: 11586406. Barykina OP, Iuzhakov VV, Chalisova NI, Kvetnoĭ IM, Konovalov SS. Sochetannoe vliianie vilona i tsiklofosfana na transplanty opukholeĭ i éksplantaty limfoidnoĭ tkani mysheĭ i krys raznogo vozrasta [Combined effect of vilon and cyclophosphane on tumor transplants and lymphoid tissue explants in mice and rats of various age]. Adv Gerontol. 2003;12:128-31. Russian. PMID: 14743610. https://pubmed.ncbi.nlm.nih.gov/14743610/ Khavinson VKh, Timofeeva NM, Malinin VV, Cordova LA, Nikitina AA. Effect of vilon and epithalon on activity of enzymes in epithelial and subepithelial layers in small intestine of old rats. Bull Exp Biol Med. 2002 Dec;134(6):562-4. https://pubmed.ncbi.nlm.nih.gov/12660839/ Khavinson VKh, Egorova VV, Timofeeva NM, Malinin VV, Cordova LA, Gromova LV. Effect of Vilon and Epithalon on glucose and glycine absorption in various regions of small intestine in aged rats. Bull Exp Biol Med. 2002 May;133(5):494-6. https://pubmed.ncbi.nlm.nih.gov/12420071/ Anisimov SV, Bokheler KR, Khavinson VKh, Anisimov VN. Studies of the effects of Vilon and Epithalon on gene expression in mouse heart using DNA-microarray technology. Bull Exp Biol Med. 2002 Mar;133(3):293-9. https://pubmed.ncbi.nlm.nih.gov/12360356/ Kuznik BI, Isakova NV, Kliuchereva NN, Maleeva NV, Pinelis IS. [Effect of vilon on the immunity status and coagulation hemostasis in patients of different age with diabetes mellitus]. Adv Gerontol. 2007;20(2):106-15. Russian. PMID: 18306698. https://pubmed.ncbi.nlm.nih.gov/18306698/ Gavrisheva NA, Malinin VV, Ses TP, Kozlov KL, Panchenko AV, Titkov AY. Effect of peptide Vilon on the content of transforming growth factor-beta and permeability of microvessels during experimental chronic renal failure. Bull Exp Biol Med. 2005 Jan;139(1):24-6. DOI: 10.1007/s10517-005-0202-9. PMID: 16142267. https://pubmed.ncbi.nlm.nih.gov/16142267/ 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.
Sermorelin & Ipamorelin Blend (10mg)
Both Ipamorelin & Sermorelin are synthetic peptides, and when blended, they may act synergistically to further their individual potential impacts. More specifically, they both appear to upregulate the production of growth hormone. The growth hormone appears to play a vital role in accelerating growth and is considered to function primarily to regulate metabolic functions. Overview Sermorelin & Ipamorelin are synthetic peptides, where Sermorelin is composed of 29 amino acids(1) and Ipamorelin is composed of 5 amino acids.(2) Sermorelin seems to serve as a functional equivalent to the naturally occurring growth hormone-releasing hormone (GHRH). Unlike GHRH, which consists of 44 amino acids, Sermorelin is shortened to a sequence of 29 amino acids. This truncated form is also referred to as Growth Hormone Releasing Factor (1-29) or simply GRF (1-29). Ipamorelin was the first synthetic GHS discovered with a proposed high selectivity towards the growth hormone receptors without apparently affecting the synthesis of other pituitary hormones such as ACTH and prolactin.(3) Sermorelin is also known as GHRF (1-29) amide, and the potential of this fragment was first investigated in the early 1980s. It was suggested that upon introduction, Sermorelin may exhibit affinity towards the GHRH receptors located at the pituitary gland and possibly stimulate the secretion of growth hormone.(4) Both Ipamorelin & Sermorelin are posited to produce action on the pituitary gland. Upon binding, these peptides are suggested to stimulate the pituitary gland and secrete more growth hormone.(4)(5) The difference in their mode of action is the pathway by which they exert their action. Sermorelin appears to affect the GHRH receptors while Ipamorelin appears to act via the ghrelin pathway.(5) Thus, it is believed that Sermorelin may retain the core ability of GHRH: to potentially prompt the GHRH receptors in the pituitary gland to intermittently release growth hormone. This action is thought to subsequently elevate levels of insulin-like growth factor-1 (IGF-1), which is viewed as the primary agent responsible for the anabolic action of growth hormone. Ipamorelin does not appear to work via the GHRH receptors. Instead, this synthetic pentapeptide is under investigation for its potential capabilities as a growth hormone secretagogue (GHS). It is thought to function similarly to Growth Hormone Releasing Peptides (GHRPs) and may potentially mimic the natural action of the hunger hormone, ghrelin. The peptide is suspected to target ghrelin receptors in the anterior pituitary gland, also known as Growth Hormone Secretagogue Receptors 1 Alpha (GHS-R1a). This characteristic positions Ipamorelin as a highly selective secretagogue and a potent agonist for the growth hormone/ghrelin secretagogue receptor. Since the mode of action of both the peptides appears to be different, they may complement each other when presented together and thereby provide a potentially greater growth hormone response. A major difference between the two peptides appears to be their respective half-lives, where the half-life of Sermorelin is considered to be 11 to 12 minutes and that of Ipamorelin is approximately 2 hours.(6) Therefore, research has posited that Sermorelin may trigger an immediate growth hormone response while Ipamorelin may extend this process for longer periods. Chemical Makeup Molecular Formula: Sermorelin: C149H246N44O42S Ipamorelin: C38H49N9O5 Molecular Weight: Sermorelin: 3357.93 g/mol Ipamorelin: 771.86 g/mol Other Known Titles Sermorelin: GRF 1-29 Ipamorelin: NNC 26-0161 Research and Clinical Studies Currently, there is no research and clinical data available for the Ipamorelin & Sermorelin blend together, however both these peptides have been individually studied. Sermorelin & Ipamorelin Blend and Growth Hormone Sermorelin and ipamorelin are both peptides that have been investigated for their possible roles in elevating levels of growth hormone and its potential anabolic mediator, IGF-1. One study seems to suggest that Sermorelin may lead to an 82% increase in average growth hormone levels, which appeared to last for around two hours.(7) Another study, lasting 16 weeks, posited that Sermorelin might potentially result in up to a 107% rise in growth hormone levels and up to a 28% uptick in IGF-1 levels.(8 Conversely, Ipamorelin has been associated with what appears to be a substantial increase in growth hormone levels, reaching levels that may be as high as 80mIU/l (approximately a 26.6ng/ml concentration). When these figures are presented as a percentage increase compared to a placebo (1.31mIU/l (0.4ng/ml)), it seems to represent a noteworthy elevation in growth hormone levels, exceeding 6000%. Both peptides appear to have a strong potential for raising growth hormone and IGF-1 levels. However, it is worth noting that the extent of the increase and the duration for which these elevated levels are maintained could vary between the two.(9 Sermorelin & Ipamorelin Blend and Lean Mass Both Sermorelin and Ipamorelin appear to exert influence on lean mass and body composition. According to research, Sermorelin has been suggested to increase lean body mass by a margin of 2.78 lbs (1.26 kg), without affecting fat mass. These observations are posited to be due to the potential of the peptide to increase growth hormone and subsequently IGF-1, a purported anabolic mediator of growth hormone.(8) The most notable results commented by the researchers included that “...a gain of 1.26 ± 0.52 kg (P < 0.05) in LBM was found.” and “Skin thickness increased significantly…” Ipamorelin has also been suggested to potentially lead to lean mass increase, related to an increase in appetite and total weight gain. That is related to the proposed impact that Ipamorelin may have on ghrelin receptors. For instance, research suggests that subjects exposed to Ipamorelin exhibited a weight increase by roughly 17%.(10) The compound is thought to potentially elevate fat pad weights in proportion to total body mass. Consequently, measurements taken via dual energy X-ray absorptiometry (DEXA) might indicate a relative increase in body fat. Moreover, there are indications that Ipamorelin may have elevated serum leptin levels, a hormone involved in energy and appetite regulation. The researchers posited that “GHSs increase body fat by GH-independent mechanisms that may include increased feeding.” This has led experts to speculate that heightened food consumption may contribute to the observed weight gain in groups presented with Ipamorelin. Sermorelin & Ipamorelin Blend and Bone Mineralization Ipamorelin has been purported to potentially cause an increase in bone mineral density which may be related to its apparent role in increasing lean and total weight. During an investigation, Ipamorelin and a placebo were tested on mouse models to evaluate their action on bone density.(11) The study utilized real-time DEXA scans to track alterations in bone mineral content, with a focus on specific areas such as the femur and L6 vertebrae. Once the study concluded, pQCT scans were performed on the femurs to gather additional data. Preliminary results suggest a potential correlation between Ipamorelin and both weight gain and an increase in bone mineral content in the tibia and vertebrae, as evidenced by DEXA, relative to the placebo group. Furthermore, the pQCT findings hint that the noted increase in cortical BMC could be due to an expansion in the bone's cross-sectional area. Sermorelin & Ipamorelin Blend is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References: National Center for Biotechnology Information. “PubChem Compound Summary for CID 16129620, Sermorelin” PubChem, https://pubchem.ncbi.nlm.nih.gov/compound/Sermorelin National Center for Biotechnology Information. “PubChem Compound Summary for CID 9831659, Ipamorelin” PubChem, https://pubchem.ncbi.nlm.nih.gov/compound/Ipamorelin Raun K, Hansen BS, Johansen NL, Thøgersen H, Madsen K, Ankersen M, Andersen PH. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998 Nov;139(5):552-61. https://pubmed.ncbi.nlm.nih.gov/9849822/ Clark, R G, and I C Robinson. “Growth induced by pulsatile infusion of an amidated fragment of human growth hormone releasing factor in normal and GHRF-deficient rats.” Nature vol. 314,6008 (1985): 281-3. https://pubmed.ncbi.nlm.nih.gov/2858818/ 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 Junichi I. et al, Growth hormone secretagogues: history, mechanism of action, and clinical development, JSCM Rapid Communications Vol. 3 Issue 1, 09 February 2020. https://onlinelibrary.wiley.com/doi/full/10.1002/rco2.9 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 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 Gobburu, J. V., Agersø, H., Jusko, W. J., & Ynddal, L. (1999). Pharmacokinetic-pharmacodynamic modeling of ipamorelin, a growth hormone releasing peptide, in human volunteers. Pharmaceutical research, 16(9), 1412–1416. https://doi.org/10.1023/a:1018955126402 Lall, S., Tung, L. Y., Ohlsson, C., Jansson, J. O., & Dickson, S. L. (2001). Growth hormone (GH)-independent stimulation of adiposity by GH secretagogues. Biochemical and biophysical research communications, 280(1), 132–138. https://doi.org/10.1006/bbrc.2000.4065 Svensson, J., Lall, S., Dickson, S. L., Bengtsson, B. A., Rømer, J., Ahnfelt-Rønne, I., Ohlsson, C., & Jansson, J. O. (2000). The GH secretagogues ipamorelin and GH-releasing peptide-6 increase bone mineral content in adult female rats. The Journal of endocrinology, 165(3), 569–577. https://doi.org/10.1677/joe.0.1650569 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.
Bronchogen (20mg)
Bronchogen, also known as AEDL, is classified among the Khavinson peptides and is has been suggested by researchers to act as a bioregulator. These are short signaling peptides which may cross through cellular and nuclear membranes to directly interact with the DNA. Bronchogen may have specific affinity for lung cells by regulating the expression of the NKX2-1, SCGB1A1, SCGB3A2, FOXA1, and FOXA2 genes.(1) Furthermore, authors comment that it may “bind preferentially with deoxyribooligonucleotides containing CNG sequence (CNG sites are targets for cytosine DNA methylation in eukaryotes).”(2) Indeed, the peptide has been suggested to potentially attenuate inflammatory reactions in the lungs of murine models with bleomycin-induced fibrosis(3) Chemical Makeup Molecular formula: C18H30N4O9 Molecular weight: 446.45 g/mol Sequence: Ala-Glu-Asp-Leu Other known titles: AEDL Research and Clinical Studies Below we have delved deep into the latest clinical and preclinical data on the potential actions of Bronchogen as seen in various research models. Bronchogen and DNA Studies have suggested that the peptide may interact with “lung cells by regulating the expression of the NKX2-1, SCGB1A1, SCGB3A2, FOXA1, and FOXA2 genes” to exert its potential actions on DNA. These actions may include reducing inflammation, promoting differentiation and preventing remodeling. (1) (4) Further, Bronchogen’s interaction with DNA may affect genetic expression. The interaction between Bronchogen and deoxyribooligonucleotides (short DNA segments) containing a CNG sequence may potentially influence gene regulation and expression due to its association with cytosine DNA methylation sites. In eukaryotes, CNG sites (where "C" denotes cytosine, "N" stands for any nucleotide including A, T, G, or C, and "G" signifies guanine) are common targets for DNA methylation, which is considered to play a pivotal role in epigenetic modulation. Methylation at cytosine residues, particularly at CpG dinucleotides, is associated with gene silencing. If Bronchogen preferentially binds to these CNG sites, it may interfere with or modulate the methylation process, thereby impacting gene expression. This interaction may influence cellular differentiation and development or alter normal cellular functions.(2) Bronchogen has been suggested to potentially increase DNA thermal stability as well. One study explored the impact of Bronchogen on the thermal stability of DNA derived from calf thymus and mouse liver, employing differential scanning microcalorimetry to analyze thermodynamic parameters during DNA melting. Bronchogen apparently elevated the melting temperature of DNA by 3.1 °C, acting as a DNA-stabilizing agent. The researchers also suggested that Bronchogen may not exhibit base specificity in its binding (non-selective for adenine-thymine or guanine-cytosine pairs), and apparently engages strongly yet sporadically with both DNA strands, primarily interacting with nitrogen bases, which is in contrast with previous suggestions that it targets CNG sites. Potential mechanisms might involve non-covalent interactions, such as hydrogen bonding or van der Waals forces, between Bronchogen and nitrogen bases. The implications of Bronchogen’s potential stabilizing effect on DNA may have relevance in the study and stabilization of DNA structures, possibly aiding in the development of strategies involving nucleic acids, or in biotechnological advancements where enhanced DNA stability is crucial. Further investigations into the structural and molecular aspects of this interaction may unveil more detailed mechanisms.(5) Bronchogen and Cell Renewal Studies suggest that the Bronchogen peptide may impact cell renewal processes and augment the functionality of bronchial epithelial cells, which opens up new potential avenues in cell regeneration research, especially related to bronchial epithelial cells. The specific binding of the peptide to DNA, notably at the guanine N7 site without visibly altering the double-helix structure, indicates a targeted interaction that might be explored further. This suggests that Bronchogen may potentially modulate cellular activities at the genetic level. However, the molecular mechanism through which Bronchogen enhances cell functionality and renewal is not fully detailed yet, making an in-depth investigation into its pharmacodynamics essential to ascertain its potential and to verify that it will not provoke unwanted mutagenic or cytotoxic effects. Furthermore, Bronchogen's potential capability to bind with DNA suggests that it may be utilized in research dedicated to developing targeted delivery systems, where the peptide might be employed to direct other compounds or agents to specific DNA sequences. This interaction and the resulting biological actions need to be extensively studied to establish the potential of Bronchogen in scientific research, considering factors like potential off-target effects, stability, and delivery mechanisms. Ultimately, the researchers commented that the “peptide proved to be an efficient agent stimulating the cell renewal processes and the enhancement of the functional activity of bronchial epithelial cells.”(6) Bronchogen and Inflammation Studies have examined the potential impact of Bronchogen, on the structural and functional aspects of bronchial epithelium, as well as the inflammatory activity within murine models. This model was generated in murine subjects through intermittent exposure to nitrogen dioxide for 60 days which is considered to damage the bronchial epithelium. The bronchial epithelium plays an essential role in guarding against inhaled noxious substances. Bronchogen, by hypothetically modulating inflammatory activity and the bronchial epithelium state in this model, may have led to a reduction in neutrophilic inflammation and normalization of the cellular composition and profile of pro-inflammatory cytokines and enzymes in the bronchoalveolar space. The researchers suggested an apparent structural and functional rejuvenation of the bronchial epithelium, indicated by increased levels of secretory immunoglobulin A, a marker for local immunity, and surfactant protein B, which modulates alveolar surface tension. Possible mechanisms related to these observations may involve Bronchogen intervening in the inflammatory cascade, possibly inhibiting pro-inflammatory cytokines and enzymes, thus alleviating inflammation. Additionally, the peptide might promote regenerative processes in the bronchial epithelium, enhancing its barrier function, and contributing to the balance of surfactant proteins essential for lung function and defenses. This research hints at novel peptide-based strategies for addressing the inflammatory and structural challenges posed by specific respiratory conditions. Further studies, particularly in broader models, are ongoing.(7) Further research suggest that these antiinflammatory actions may be exerted on the bronchial epithelium state to prevent fibrotic changes in the lungs but that the peptide may have potentially beneficial actions in other areas such as minimizing hemodynamic disturbances and possibly reducing myocardial hypertrophy in experimental models.(3) Bronchogen and Tissue Remodeling Trials have investigated the potential of Bronchogen for preventing tissue remodeling in murine models which went through 60-day intermittent exposure to NO2. Bronchogen appeared to abate typical symptoms of bronchial epithelium and lung tissue remodeling, such as goblet cell hyperplasia, squamous metaplasia, lymphocytic infiltration, and emphysema, while also potentially restoring ciliated cells. The researchers commented that there may be an increase in secretory IgA production, indicative of normalized functional activity of bronchial epithelium, and stabilization of cell composition and proinflammatory cytokine profile in the bronchoalveolar space, hinting at reduced neutrophilic inflammation. These outcomes suggest that Bronchogen might alleviate the physical restructuring and dysfunction of lung tissues but also potentially reverse these alterations. The enhanced production of secretory IgA and the modulation of inflammatory markers suggest a mechanism involving immune enhancement and inflammation control.(8) NOTE: These products are intended for laboratory research use only. This peptide is not intended for personal use. Please review and adhere to our Terms and Conditions before ordering. References: 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 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.h, Linkova, N. S., Polyakova, V. O., Kheifets, O. V., Tarnovskaya, S. I., & Kvetnoy, I. M. (2012). Peptides tissue-specifically stimulate cell differentiation during their aging. Bulletin of experimental biology and medicine, 153(1), 148–151. https://doi.org/10.1007/s10517-012-1664-1 Caputi, S., Trubiani, O., Sinjari, B., Trofimova, S., Diomede, F., Linkova, N., Diatlova, A., & Khavinson, V. (2019). Effect of short peptides on neuronal differentiation of stem cells. International journal of immunopathology and pharmacology, 33, 2058738419828613. https://doi.org/10.1177/2058738419828613 Monaselidze, J. R., Khavinson, V. K.h, Gorgoshidze, M. Z., Khachidze, D. G., Lomidze, E. M., Jokhadze, T. A., & Lezhava, T. A. (2011). Effect of the peptide bronchogen (Ala-Asp-Glu-Leu) on DNA thermostability. Bulletin of experimental biology and medicine, 150(3), 375–377. https://doi.org/10.1007/s10517-011-1146-x Morozova, E. A., Lin’kova, N. S., Khavinson, V. K., Soloviev, A. Y., & Kasyanenko, N. A. (2017). In vitro interaction of the AEDL peptide with DNA. Journal of Structural Chemistry, 58, 420-424. Titova, O. N., Kuzubova, N. A., Lebedeva, E. S., Preobrazhenskaya, T. N., Surkova, E. A., & Dvorakovskaya, I. V. (2017). Rossiiskii fiziologicheskii zhurnal imeni I.M. Sechenova, 103(2), 201–208. Kuzubova, N. A., Lebedeva, E. S., Dvorakovskaya, I. V., Surkova, E. A., Platonova, I. S., & Titova, O. N. (2015). Modulating Effect of Peptide Therapy on the Morphofunctional State of Bronchial Epithelium in Rats with Obstructive Lung Pathology. Bulletin of experimental biology and medicine, 159(5), 685–688. https://doi.org/10.1007/s10517-015-3047-x Dr. MarinovDr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.
N-Acetyl Selank (10mg)
N-Acetyl Selank is a short, synthetic heptapeptide analogous to the naturally occurring peptide called Tuftsin.(1) Tuftsin is an endogenous tetrapeptide that appears to regulate the immune system. Selank peptide may exhibit immunomodulatory potential; however, it has also been studied in models of anxiety and cognitive decline for its nootropic potential. Apart from the homology with tuftsin, the peptide appears to have a Pro-Gly-Pro fragment at its C-terminus, which may provide an enhancement of Selank's potential to traverse through different tissues and models including the blood-brain barrier (BBB). The BBB is a highly selective, semi-permeable border that separates the circulating blood from the tissues and extracellular fluid in the central nervous system, and is considered to play a crucial role in regulating the passage of substances. Pro-Gly-Pro addition might enhance BBB permeability by potentially impacting the peptide's overall hydrophilicity or lipophilicity, thereby increasing its affinity for the lipid-rich environment of the BBB. Additionally, the Pro-Gly-Pro sequence may interact with specific transport mechanisms or receptors at the BBB, potentially triggering a facilitated transport or receptor-mediated endocytosis. Such processes might allow Selank to bypass the tight junctions that normally restrict the passage of large molecules. Pro-Gly-Pro fragment may also influence the peptide's tertiary structure in a way that makes it more conducive to crossing the BBB. Further, N-Acetyl Selank Amidate has an additional acetyl group attached to the N-terminus. Adding an acetyl group to the N-terminus in N-Acetyl Selank Amidate may improve the peptide's stability through several speculative mechanisms. Acetylation might potentially shield the peptide from rapid enzymatic degradation by exopeptidases, as it might make the N-terminus less accessible or recognizable to these enzymes. Additionally, acetylation may induce changes in the peptide's structure, possibly leading to a more stable conformation that resists denaturation. Overview Studies suggest that the Selank peptide produces possible action in several ways: Firstly, by potentially stimulating the gamma-aminobutyric acid (GABA) receptors system.(2) GABA is considered an inhibitory neurotransmitter in the brain, reducing neuronal excitability, promoting relaxation, and alleviating anxiety. Researchers have posited Selank to potentiate the capacity to induce changes in the expression of genes associated with GABA receptors, transporters, and ion channels. This implies that Selank might potentially influence GABAergic neurotransmission by modulating the availability or functionality of these key components. Furthermore, studies posit that Selank's actions may potentially extend beyond direct actions on GABA receptor gene expression to allosteric modulation of the GABAergic system. This is hinted at by the differential gene expression patterns observed following Selank and GABA exposure, wherein Selank appeared to have uniquely influenced the expression of certain genes. This nuanced action suggests that Selank may modulate the GABAergic system's function in a manner distinct from the straightforward receptor activation induced by GABA. Selank might also initiate longer-lasting alterations in neurotransmitter systems, potentially explaining its prolonged anxiolytic actions in experimental models. Secondly, the peptide may potentially interact with serotonin signaling.(3) Serotonin signaling in the brain is posited to regulate mood and anxiety. Experiments in murine models with blocked serotonin synthesis suggest that Selank may exert the potential to modulate serotonin levels under compromised serotonergic function. Selank was posited to enhance serotonin metabolism in the brainstem via a rapid onset of action on the serotonin system. Specifically, the peptide was suggested to promote increased metabolic activity of serotonin in parts of the brain linked to regulating mood and anxiety. Further, the study posits that Selank's potential to elevate serotonin metabolism indicates a possible mechanism through which Selank might correct disturbances associated with reduced serotonin function. Thirdly, the peptide may act by potentially modulating enkephalin signaling.(4)(5) Studies have posited that Selank may have an inhibitory action on enkephalin-degrading enzymes. This indicates that Selank might slow down the degradation of enkephalins. Enkephalins, as natural ligands of opioid receptors, are considered to play a role in pain perception and modulating mood and stress, implying that Selank’s action on these enzymes might enhance the availability of enkephalins, thereby potentially amplifying their actions. Studies also posit that there may be a tau(1/2) leu-enkephalin increase during Selank exposure in anxiety models. Finally, the peptide may potentially affect brain-derived neurotrophic factor (BDNF) expression.(8) Selank has been suggested to significantly elevate BDNF mRNA levels in the hippocampus, a part of the central nervous system. Selank's potential to enhance BDNF expression, especially in the context of stress and glucocorticoid-induced suppression of BDNF, points towards its potential research implications for ameliorating reduced neuroplasticity. Furthermore, researchers are currently investigating the potential actions of the peptide via genome expression and involvement in the inflammatory process.(7) Chemical Makeup(8) Molecular Formula: C33H57N11O9 Molecular Weight: 751.9 g/mol Other known titles: TP-7, Selanc Research and Clinical Studies Unfortunately, research on N-Acetyl Selank in its acetylated form is still sparse. However, the peptide is expected to have similar impacts as its unacetylated counterpart, Selank, with the addition possibly only affecting the peptide by providing higher stability. Because of this lack of research data, we cite only Selank studies below. N-Acetyl Selank and Anxiolytic Action In 2008, a clinical study(5) was conducted on research models of generalized anxiety disorder (GAD). The research models were divided into two groups – half were presented with allopathic anxiety compounds, and the other half were presented with Selank peptide. After completing this study, the psychometric levels of all models were examined. Based on the results, it was suggested that the Selank peptide appeared to be potentially as impactful as the control compound in reducing the models’ anxiety levels. The peptide-exposed group also exhibited reportedly positive psychostimulant reactions. As per A A Zozulia et al., “The clinical-biological study revealed that [models] with GAD and neurasthenia had the decreased level of tau(1/2) leu-enkephalin [...]. The increase of this parameter and stronger positive correlations with anxiety level were observed during the [exposure to] Selank.” N-Acetyl Selank and Anxiety In this clinical study,(9) research models of standard anxiety and phobia thresholds were examined. The research models were separated into an experimental and control group; the controls were exposed to an allopathic compound, and the experimental group was exposed to Selank peptide. After this study's completion, the results appeared to indicate the peptide's anxiolytic and nootropic potential. N-Acetyl Selank and Mental Cognition Research studies(10) evaluated experimental murine models following exposure to Selank peptide, after which the mice underwent ‘training’ exercises for four days to learn conditioned avoidance response (CAR). Observing the behavior of the models throughout the training period, researchers observed that the learning abilities of murine models appeared to improve as the number of errors reduced over time, compared to control models under the same conditions. These researchers suggested that the peptide may have exhibited nootropic potential. It is posited that such actions on learning and memory might involve several interconnected mechanisms, such as the modulation of neuropeptide systems in the brain, leveraging the potential role these peptides may play in cognitive functions to enhance learning and memory processes. Further, Selank may influence the neural pathways associated with memory consolidation, possibly improving synaptic stability and efficiency, deemed essential for learning. Selank might also facilitate cognitive performance indirectly by reducing anxiety-related parameters, which may often hinder learning efficiency, suggesting a role in the affective components of cognition. The peptide may also have the unique potential to enhance neural plasticity or resilience in underperforming cognitive circuits, thereby improving their functionality. N-Acetyl Selank and Immunomodulation Research models of anxiety and neurasthenia were evaluated in this study(11) following routine exposure to Selank for two weeks. After two weeks, blood samples were collected and analyzed. It was reported that there was a significant rise in the levels of interleukin-6 cytokines and alteration in the Th1 to Th2 cytokine ratio. As per O.N. Uchakina et al., "The cytokine regulating effects revealed in the study suggest that Selank [might act as] a novel immunomodulator in … anxiety-asthenic disorders. Additionally, the adaptogenic properties of Selank may benefit … environmental stressors to prevent infectious diseases.” N-Acetyl Selank and Substance Withdrawal A study(12) in experimental murine models infused the animals with 10% ethanol for 24 weeks. Upon discontinuing alcohol infusion, these murine models exhibited significant alcohol withdrawal symptoms. At this time, the peptide was then given to all affected murine models. 48 hours after the peptide, it was suggested by the researchers that the alcohol withdrawal symptoms were reportedly reduced in all murine models. N-Acetyl Selank and Cholesterol Control In one study,(13) murine models were subjected to a high-fat diet for six consecutive weeks until they gained a standard set weight. At that time, the models were divided into two groups – one exposed to a sodium chloride solution and the rest to the Selank peptide. Upon analysis, it was observed that the peptide group exhibited apparently improved fat metabolism, with a reported reduction of cholesterol levels up to 58%. Most notably, the researchers suggested that Selank may potentially decrease total cholesterol, low-density lipoprotein (LDL), very-low-density lipoprotein (VLDL) cholesterol, and triglycerides. This suggests Selank may have either a direct or indirect role in modulating lipid metabolism and may possibly exhibit hypocholesterolemic and/or hypolipidemic action. Furthermore, the study observed apparent improvements in hemostasis parameters, such as increased total fibrinolytic activity and a reduction in platelet aggregation, which might imply amelioration of prothrombotic states. The research also hints at a potential regulatory action of Selank on glucose homeostasis. N-Acetyl Selank peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References Kozlovskaya MM, Kozlovskii II, Val'dman EA, Seredenin SB. Selank and short peptides of the tuftsin family in the regulation of adaptive behavior in stress. Neurosci Behav Physiol. 2003 Nov;33(9):853-60. https://pubmed.ncbi.nlm.nih.gov/14969422/ Volkova, A., Shadrina, M., Kolomin, T., Andreeva, L., Limborska, S., Myasoedov, N., & Slominsky, P. (2016). Selank Administration Affects the Expression of Some Genes Involved in GABAergic Neurotransmission. Frontiers in pharmacology, 7, 31. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4757669/ Semenova, T. P., kozlovskiĭ, I. I., Zakharova, N. M., & Kozlovskaia, M. M. (2009). Eksperimental'naia i klinicheskaia farmakologiia, 72(4), 6–8. Kost, N. V., Sokolov, O. I.u, Gabaeva, M. V., Grivennikov, I. A., Andreeva, L. A., Miasoedov, N. F., & Zozulia, A. A. (2001). Ingibiruiushchee deĭstvie semaksa i selanka na énkefalindegradiruiushchie fermenty syvorotki krovi cheloveka [Semax and selank inhibit the enkephalin-degrading enzymes from human serum]]. Bioorganicheskaia khimiia, 27(3), 180–183. https://doi.org/10.1023/a:1011373002885 Zozulia, A. A., Neznamov, G. G., Siuniakov, T. S., Kost, N. V., Gabaeva, M. V., Sokolov, O. I.u, Serebriakova, E. V., Siranchieva, O. A., Andriushenko, A. V., Telesheva, E. S., Siuniakov, S. A., Smulevich, A. B., Miasoedov, N. F., & Seredenin, S. B. (2008). Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova, 108(4), 38–48. Inozemtseva, L. S., Karpenko, E. A., Dolotov, O. V., Levitskaya, N. G., Kamensky, A. A., Andreeva, L. A., & Grivennikov, I. A. (2008). Intranasal administration of the peptide Selank regulates BDNF expression in the rat hippocampus in vivo. Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections, 421, 241–243. https://doi.org/10.1134/s0012496608040066 T.A Kolomin et al., Transcriptomic Response of Rat Hippocampus and Spleen Cells to Single and Chronic Administration of the Peptide Selank. June 2, 2009. National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 11765600, Selank. https://pubchem.ncbi.nlm.nih.gov/compound/Selank Medvedev VE, Tereshchenko ON, Israelian AIu, Chobanu IK, Kost NV, Sokolov OIu, Miasoedov NF. A comparison of the anxiolytic effect and tolerability of selank and phenazepam in the treatment of anxiety disorders. Zh Nevrol Psikhiatr Im S S Korsakova. 2014;114(7):17-22. Russian. https://pubmed.ncbi.nlm.nih.gov/25176261/ Kozlovskii II, Danchev ND. The optimizing action of the synthetic peptide Selank on a conditioned active avoidance reflex in rats. Neurosci Behav Physiol. 2003 Sep;33(7):639-43. https://pubmed.ncbi.nlm.nih.gov/14552529/ Uchakina ON, Uchakin PN, Miasoedov NF, Andreeva LA, Shcherbenko VE, Mezentseva MV, Gabaeva MV, Sokolov OIu, Zozulia AA, Ershov FI. Immunomodulatory effects of selank in patients with anxiety-asthenic disorders. Zh Nevrol Psikhiatr Im S S Korsakova. 2008;108(5):71-5. Russian. https://pubmed.ncbi.nlm.nih.gov/18577961/ Kolik LG, Nadorova AV, Kozlovskaya MM. Efficacy of peptide anxiolytic selank during modeling of withdrawal syndrome in rats with stable alcoholic motivation. Bull Exp Biol Med. 2014 May;157(1):52-5. https://pubmed.ncbi.nlm.nih.gov/24913576/ N.F. Mjasoedov et al, The Influence of Selank on the Parameters of the Hemostasis System, Lipid Profile, and Blood Sugar Level in the Course of Experimental Metabolic Syndrome. April 14, 2014. 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.
N-Acetyl Semax (25mg)
N-Acetyl Semax is a synthetic polypeptide analogous to the naturally occurring adrenocorticotropic hormone (ACTH). The peptide is similar to a fragment from the adrenocorticotropic hormone ACTH (4-7), specifically Met-Glu-His-Phe, combined with a Pro-Gly-Pro extension at the C-terminus.(1) The addition of Pro-Gly-Pro (PGP) to N-Acetyl Semax might enable an enhanced permeability through the blood-brain barrier (BBB) by increasing the peptide's lipophilicity via improving passive diffusion or uptake via lipid raft-mediated endocytosis, which may potentially allow it to bypass the tight junctions of the BBB. The PGP addition at the C-terminus might also alter the peptide's interaction with specific BBB transporters or receptors, possibly promoting receptor-mediated transcytosis. Additionally, the acetylation of the peptide might increase its resistance to enzymatic degradation, prolonging its half-life in experimental models. Overview N-Acetyl Semax appears to exhibit potential nootropic (memory enhancing) and neuroprotective characteristics, which researchers have proposed may be produced via several routes: By potentially interacting with dopamine, serotonin, enkephalin, and brain-derived neurotrophic (BDNF) levels;(2)(3) Or by potentially modulating gene expression and increasing the efficacy of the immune system.(4) Based on studies suggesting that the peptide may inhibit serum enkephalin-degrading enzymes, it is plausible to hypothesize about the interactions between Semax and enkephalins. Researchers suggest Semax's inhibitory potential on enkephalin-degrading enzymes may lead to an increase in the levels of enkephalins by preventing their degradation. Enkephalins are endogenous opioids that are considered to play roles in nociception and stress response. Further, an increase in enkephalin levels might also influence other neurotransmitter systems due to the complex interplay between the opioid system and neurotransmitters like dopamine and serotonin.(2) According to studies, Semax may potentially increase the striatal levels of 5-hydroxyindoleacetic acid (5-HIAA), a serotonin metabolite, suggesting a possible enhancement of serotonergic activity. This potential action on serotonin metabolism might amplify serotonin-mediated pathways, possibly influencing central nervous system functioning. On the other hand, Semax does not appear to directly alter dopamine levels or its metabolites. Still, it may modulate the dopaminergic system's responsiveness, enhancing the dopaminergic agonists' action.(5) Chemical Makeup(6) Molecular Formula: C37H51N9O10S Molecular Weight: 858.97 g/mol Other known titles: ACTH (4-7)PGP, HY-P1146 Research and Clinical Studies N-Acetyl Semax and Nootropic Potential A study(5) was conducted on experimental rodents to determine the nootropic potential of ACTH hormone and its analogs, such as Semax. After exposure to Semax, all tested rodents were examined for 5-hyrodxyindoleacetic acid (5-HIAA) levels. Based on the results, it was noted that the 5-HIAA levels increased by 25% after just 2 hours following exposure; they increased progressively up to a maximum of 180% after 4 hours. As per Kirill O Eremin et al., “Our results reveal the positive modulatory [action] of Semax on the striatal serotonergic system and the ability of Semax to enhance both the striatal release of dopamine and locomotor behavior elicited by D-amphetamine.” In another research study,(7) experimental models under excessive stress conditions were exposed to Semax. Upon analyzing behavior 24 hours after peptide exposure, it was noted that they appeared to show signs of enhanced memory and attention. As per the reports, "In the majority of cases, the peptide exhibited positive [actions], and in no case did it produce negative side actions or complications connected with its administration. There is good reason to believe that … potentialities of Semax have not been exhausted and in the future new possibilities … will be revealed." The study is shared here for educational and research purposes, and studies on the Semax peptide are still being conducted. N-Acetyl Semax and SSRI Interaction Selective Serotonin reuptake inhibitors (SSRIs) are a class of antidepressants. In pregnant research models, the compounds may risk passing through the placenta and impacting fetal brain development. In a preclinical research study,(8) experimental rats aged between 1 and 14 days were presented first with an SSRI compound, followed by the Semax peptide. After 4 weeks, it was observed that the rats exposed to SSRIs showcased anxious behavior, especially when exposed to new stimuli. When they were given the Semax peptide, these same rats later reportedly exhibited a reduction in their anxiety levels and potential enhancement in their learning abilities. N-Acetyl Semax and Separation Anxiety Young offspring face separation anxiety when they are away from their mothers. Separating for a prolonged period may lead to impaired emotional reactivity. A research study(9) examined young rats facing maternal deprivation. After four weeks of separation from their mothers, these rats reportedly exhibited increased anxiety and excessive physical activity. When the rats were presented with Semax, their reactions improved, indicating reduced anxiety. As per M. A. Volodina et al., these results suggest that “Semax [weakens] the impact of deprivation on animal body weight and [normalizes] the levels of anxiety in rats.” N-Acetyl Semax and the Cardiovascular System For this study,(10) rodents were induced with myocardial infarction (MI), which may lead to vascular damage. These rodents were then divided into two groups – one was given Semax peptide for six days, and the second was given a placebo. Following 28 days after the occurrence of myocardial infarction, it was reported by the researchers that the control rodents appeared to exhibit reduced arterial blood pressure and cardiac hypertrophy, both of which may signal impending heart failure. In contrast, the peptide-exposed rodents reportedly exhibited signs of prevention of diastolic blood pressure, which may indicate possible remodeling of the heart ventricle and inhibition of heart failure. N-Acetyl Semax and Neuroprotection In a clinical study,(11) research models of ischemic strokes were evaluated for 10 days. Of these, 30% were presented with conventional compounds and the Semax peptide, while the remaining 70% were presented with conventional compounds only. After 10 days, all models were examined via electroencephalogram (EEG). Based on the EEG mapping, the researchers reported that the experimental group exposed to both the peptide and compound exhibited apparently notable improvement in restoring damaged brain activity. N-Acetyl Semax peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References T. Kolomin et al., A New Generation of Drugs: Synthetic Peptides based on Natural Regulatory peptides. Neuroscience & Medicine, 2013, 223-252. Published Online December 2013. http://dx.doi.org/10.4236/nm.2013.44035 Kost NV, Sokolov OIu, Gabaeva MV, Grivennikov IA, Andreeva LA, Miasoedov NF, Zozulia AA. Ingibiruiushchee deĭstvie semaksa i selanka na énkefalindegradiruiushchie fermenty syvorotki krovi cheloveka [Semax and selank inhibit the enkephalin-degrading enzymes from human serum]]. Bioorg Khim. 2001 May-Jun;27(3):180-3. Russian. doi: 10.1023/a:1011373002885. PMID: 11443939. https://pubmed.ncbi.nlm.nih.gov/11443939/ Shih-Jen Tsai, Semax, an analogue of adrenocorticotropin (4–10), is a potential agent for the treatment of attention-deficit hyperactivity disorder and Rett syndrome, Medical Hypotheses, Volume 68, Issue 5, 2007, Pages 1144-1146. https://doi.org/10.1016/j.mehy.2006.07.017 Medvedeva, E.V., Dmitrieva, V.G., Povarova, O.V. et al. The peptide semax affects the expression of genes related to the immune and vascular systems in rat brain focal ischemia: genome-wide transcriptional analysis. BMC Genomics 15, 228 (2014). https://doi.org/10.1186/1471-2164-15-228 Eremin KO, Kudrin VS, Saransaari P, Oja SS, Grivennikov IA, Myasoedov NF, Rayevsky KS. Semax, an ACTH(4-10) analogue with nootropic properties, activates dopaminergic and serotoninergic brain systems in rodents. Neurochem Res. 2005 Dec;30(12):1493-500. doi: 10.1007/s11064-005-8826-8. PMID: 16362768. https://pubmed.ncbi.nlm.nih.gov/16362768/ National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 9811102, Semax. Asmarin IP, Nezavibat'ko VN, Miasoedov NF, Kamenskiĭ AA, Grivennikov IA, Ponomareva-Stepnaia MA, Andreeva LA, Kaplan AIa, Koshelev VB, Riasina TV. Nootropnyĭ analog adrenokortikotropina 4-10-semaks (15-letniĭ opyt razrabotki i izucheniia) [A nootropic adrenocorticotropin analog 4-10-semax (l5 years experience in its design and study)]. Zh Vyssh Nerv Deiat Im I P Pavlova. 1997 Mar-Apr;47(2):420-30. Russian. PMID: 9173745. https://pubmed.ncbi.nlm.nih.gov/9173745/ Nataliya Yu. Glazova, Daria M. Manchenko, Maria A. Volodina, Svetlana A. Merchieva, Ludmila A. Andreeva, Vladimir S. Kudrin, Nikolai F. Myasoedov, Natalia G. Levitskaya, Semax, synthetic ACTH(4–10) analog, attenuates behavioural and neurochemical alterations following early-life fluvoxamine exposure in white rats, Neuropeptides, Volume 86, 2021, 102114, ISSN 0143-4179. https://doi.org/10.1016/j.npep.2020.102114 Volodina MA, Sebentsova EA, Glazova NY, Levitskaya NG, Andreeva LA, Manchenko DM, Kamensky AA, Myasoedov NF. Semax attenuates the influence of neonatal maternal deprivation on the behavior of adolescent white rats. Bull Exp Biol Med. 2012 Mar;152(5):560-3. English, Russian. doi: 10.1007/s10517-012-1574-2. PMID: 22803132. https://pubmed.ncbi.nlm.nih.gov/22803132/ Gavrilova SA, Golubeva AV, Lipina TV, Fominykh ES, Shornikova MV, Postnikov AB, Andrejeva LA, Chentsov IuS, Koshelev VB. [Protective effect of peptide semax (ACTH(4-7)Pro-Gly-Pro) on the rat heart rate after myocardial infarction]. Ross Fiziol Zh Im I M Sechenova. 2006 Nov;92(11):1305-21. Russian. PMID: 17385423. https://pubmed.ncbi.nlm.nih.gov/17385423/ Gusev EI, Skvortsova VI, Miasoedov NF, Nezavibat'ko VN, Zhuravleva EIu, Vanichkin AV. Effektivnost' semaksa v ostrom periode polusharnogo ishemicheskogo insul'ta (klinicheskoe i élektrofiziologicheskoe issledovanie) [Effectiveness of semax in acute period of hemispheric ischemic stroke (a clinical and electrophysiological study)]. Zh Nevrol Psikhiatr Im S S Korsakova. 1997;97(6):26-34. Russian. PMID: 11517472. https://pubmed.ncbi.nlm.nih.gov/11517472/ 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 & Ipamorelin Blend (10mg)
The Ipamorelin peptide has been studied for its potential as a growth hormone secretagogue (GHS). This synthetic pentapeptide is thought to operate in a manner akin to Growth Hormone Releasing Peptides (GHRPs) and may simulate the natural action of the hunger hormone, ghrelin. Specifically, it is believed that Ipamorelin may activate ghrelin receptors in the anterior pituitary gland, also known as Growth Hormone Secretagogue Receptors 1 Alpha (GHS-R1a). This makes it a notably selective secretagogue and a strong agonist for the growth hormone/ghrelin secretagogue receptor. What sets Ipamorelin apart is its selectivity, as it does not appear to influence the release of other hormones from the pituitary gland, such as prolactin, follicle-stimulating hormone (FSH), luteinizing hormone (LH), thyroid-stimulating hormone (TSH), or Adrenocorticotropic hormone (ACTH). Modified GRF (1-29) peptide, also known as Mod GRF 1-29, is a synthetic analog of natural growth hormone-releasing hormone (GHRH). Comprising the initial 29 amino acids of the native hormone, this analog appears to stimulate GHRH receptors located in the somatotroph cells of the anterior pituitary gland, thereby facilitating the release of growth hormone. While it shares structural similarities with GRF 1-29, Mod GRF 1-29 has been slightly altered by replacing four amino acids in its original sequence. These adjustments seem to improve the peptide's pharmacokinetic properties. When presented together as a blend, these peptides appear to yield synergistic results, possibly stimulating the pituitary gland and triggering the release of growth hormone. Chemical Makeup (1)(2)(3) Molecular Formula: Modified GRF 1-29: C152H252N44O42 Ipamorelin: C38H49N9O5 Molecular Weight: Modified GRF 1-29: 3367.95 g/mol Ipamorelin: 711.86 g/mol Other Known Titles Modified GRF 1-29: Mod GRF 1-29, CJC-1295 without DAC Ipamorelin: Ipamorelin Acetate, Aib-His-D-2-Nal-D-Phe-Lys-NH2 Research and Clinical Studies Mod GRF 1-29 & Ipamorelin Blend General Research A 1998 study(4) was carried out where these growth hormone secretagogues were presented in the rat pituitary gland as well as in anesthetized rats and conscious swine. Results of all three studies suggested that these peptides are agonists of GHRP-like receptors, as they bind to these receptors and help secrete higher concentrations of growth hormone. While some growth hormone secretagogues also appeared to trigger increased levels of other hormones such as cortisol and ACTH, Ipamorelin and Modified GRF 1-29 peptides appeared to exhibit selectivity towards growth hormones only, suggesting that these peptides may be particular in their functions. In one 1999 clinical study,(5) eight test subjects were enrolled to examine the potential of growth hormone secretagogues at different concentrations. The concentrations were increased every 15 minutes for up to two hours. After the study was completed, the concentration of growth hormones appeared to have significantly risen throughout the study period. Mod GRF 1-29 & Ipamorelin Blend and Potency In this preliminary study,(6) experimental rats were examined after being introduced to GHRH peptide analogs such as Modified GRF 1-29 peptide. The results suggested that the peptide may be considerably more potent than regular GRF 1-29. Mod GRF 1-29 & Ipamorelin Blend and the Pituitary When Mod GRF 1-29 interacts with GHRH receptors on the somatotroph cells of the anterior pituitary gland, it is theorized to act as a catalyst for ensuing cellular activities that may contribute to the release of growth hormone. This interaction is thought to set off a chain of intracellular signaling events. One such signaling route that seems to be engaged is the adenylyl cyclase pathway, potentially leading to the transformation of ATP (adenosine triphosphate) into cAMP (cyclic adenosine monophosphate).(7) The subsequent elevation in cAMP levels is speculated to activate protein kinase A (PKA), which in turn may result in the phosphorylation of various proteins. Among these proteins are the voltage-dependent calcium channels located on the cell membrane. The phosphorylation of these channels is conjectured to facilitate the influx of calcium ions into the somatotrophic cells. Elevated levels of intracellular calcium are considered to be a key factor in the subsequent stages that may lead to growth hormone release. It is further theorized that these high calcium concentrations within the cell could prompt the secretory vesicles in the somatotroph cells to release growth hormone into the bloodstream. It seems that Ipamorelin may also engage with cells in the front part of the pituitary gland by targeting the N-terminal region of GHS-R1a. This region contains specific binding sites that are likely sensitive to particular sequences in the secretagogue. When Ipamorelin encounters this receptor, it may form a temporary bond, facilitated by hydrogen bonds and van der Waals interactions. This transient bonding may induce a conformational change in the receptor, potentially triggering intracellular signaling pathways, predominantly those associated with G-proteins.(8) Specifically, GHS-R1a is thought to collaborate with a specialized subunit of G-proteins known as Gαq/11. Gαq/11 is believed to interact with PLC, which may then cleave a lipid molecule called phosphatidylinositol 4,5-bisphosphate (PIP2) into two secondary messengers: IP3 (Inositol trisphosphate) and DAG (Diacylglycerol). IP3 may bind to specific sites on an organelle known as the endoplasmic reticulum, possibly leading to the release of calcium ions (Ca2+) and activation of proteins that facilitate the secretion of growth hormone from pituitary cells.(9) Mod GRF 1-29 & Ipamorelin Blend and the Gastrointestinal System In a particular study, scientists explored how Ipamorelin might influence gastric function, specifically focusing on its potential to accelerate gastric emptying. They used a specialized method to measure gastric emptying, which involves tracking the percentage of radioactivity remaining in the stomach 15 minutes after introducing a specific substance via intragastric gavage. The team noted that the surgical procedures performed on the abdomen could have contributed to a slower rate of gastric emptying, especially evident in the control group that received a vehicle substance. Contrastingly, Ipamorelin seemed to significantly hasten the emptying process when compared to the control group. This led the researchers to consider the possibility that Ipamorelin could enhance the speed of gastric emptying. Further investigations were carried out to understand the compound's impact on the contractile behavior of gastric smooth muscles, which were stimulated by acetylcholine and electrical field stimulation. The findings indicated that surgical intervention and manipulation of the intestines might substantially suppress the contractile responses of these muscles to both stimuli. Interestingly, this suppression appeared to be counteracted when both Ipamorelin and ghrelin were introduced together. This raises the speculative notion that Ipamorelin may not only stimulate the contractility of gastric smooth muscles but also potentially negate the inhibitory action induced by certain surgical procedures.(10) Mod GRF 1-29 & Ipamorelin Blend and Appetite The potential impact of Ipamorelin on ghrelin receptors suggests it may possibly boost appetite and, maybe, contribute to weight gain. A study indicates that experimental subjects experienced an approximate 15% increase in body weight when exposed to Ipamorelin.(11) Researchers theorize that this compound may have proportionally increased fat pad weights relative to overall body mass.(11) As a result, dual-energy X-ray absorptiometry (DEXA) measurements may show a relative uptick in body fat. Additionally, data suggests that Ipamorelin may have raised levels of serum leptin, a hormone implicated in regulating energy and appetite. This leads scientists to hypothesize that increased food intake may be a factor in the observed weight gain among the Ipamorelin groups. They commented that “GHSs increase body fat by GH-independent mechanisms that may include increased feeding.” Mod GRF 1-29 & Ipamorelin Blend and Bone Density In a study involving murine models, Ipamorelin and a control substance were introduced to assess their potential on bone mass. Real-time DEXA was employed to monitor changes in bone mineral content, focusing on specific regions like the femur and L6 vertebrae. After the research period, mid-diaphyseal peripheral quantitative computed tomography (pQCT) scans were conducted on the femurs of the subjects. Initial findings indicate that Ipamorelin may be linked to a potential increase in weight as well as a possible uptick in bone mineral content in the tibia and vertebrae, as revealed by DEXA, when compared to the control group. Moreover, pQCT data suggests that the observed rise in cortical BMC may be attributable to an enlargement in the bone's cross-sectional area.(12) The researchers also posited that “small stimulatory effects on linear bone growth may not have been detected statistically in the GH- and ipamorelin-treated groups,” Mod GRF 1-29 & Ipamorelin Blend is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 91976842, CJC1295 Without DAC. https://pubchem.ncbi.nlm.nih.gov/compound/CJC1295-Without-DAC. National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 9831659, Ipamorelin. https://pubchem.ncbi.nlm.nih.gov/compound/Ipamorelin. Jetté L, Léger R, Thibaudeau K, Benquet C, Robitaille M, Pellerin I, Paradis V, van Wyk P, Pham K, Bridon DP. Human growth hormone-releasing factor (hGRF)1-29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: identification of CJC-1295 as a long-lasting GRF analog. Endocrinology. 2005 Jul;146(7):3052-8. doi: 10.1210/en.2004-1286. Epub 2005 Apr 7. PMID: 15817669. https://pubmed.ncbi.nlm.nih.gov/15817669/ Raun K, Hansen BS, Johansen NL, Thøgersen H, Madsen K, Ankersen M, Andersen PH. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998 Nov;139(5):552-61. doi: 10.1530/eje.0.1390552. PMID: 9849822. https://pubmed.ncbi.nlm.nih.gov/9849822/ Gobburu, J.V.S., Agersø, H., Jusko, W.J. et al. Pharmacokinetic-Pharmacodynamic Modeling of Ipamorelin, a Growth Hormone Releasing Peptide, in Human Volunteers. Pharm Res 16, 1412–1416 (1999). https://doi.org/10.1023/A:1018955126402 Schally AV, Zhang X, Cai R, Hare JM, Granata R, Bartoli M. Actions and Potential Therapeutic Applications of Growth Hormone-Releasing Hormone Agonists. Endocrinology. 2019 Jul 1;160(7):1600-1612. https://pubmed.ncbi.nlm.nih.gov/31070727/ 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 Yin, Y., Li, Y., & Zhang, W. (2014). The growth hormone secretagogue receptor: its intracellular signaling and regulation. International journal of molecular sciences, 15(3), 4837–4855. https://doi.org/10.3390/ijms15034837 Bill, C. A., & Vines, C. M. (2020). Phospholipase C. Advances in experimental medicine and biology, 1131, 215–242. https://doi.org/10.1007/978-3-030-12457-1_9 Greenwood-Van Meerveld, B., Tyler, K., Mohammadi, E., & Pietra, C. (2012). Efficacy of ipamorelin, a ghrelin mimetic, on gastric dysmotility in a rodent model of postoperative ileus. Journal of experimental pharmacology, 4, 149–155. https://doi.org/10.2147/JEP.S35396 Lall, S., Tung, L. Y., Ohlsson, C., Jansson, J. O., & Dickson, S. L. (2001). Growth hormone (GH)-independent stimulation of adiposity by GH secretagogues. Biochemical and biophysical research communications, 280(1), 132–138. https://doi.org/10.1006/bbrc.2000.4065 Svensson, J., Lall, S., Dickson, S. L., Bengtsson, B. A., Rømer, J., Ahnfelt-Rønne, I., Ohlsson, C., & Jansson, J. O. (2000). The GH secretagogues ipamorelin and GH-releasing peptide-6 increase bone mineral content in adult female rats. The Journal of endocrinology, 165(3), 569–577. https://doi.org/10.1677/joe.0.1650569 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.
CJC-1295 & GHRP-6 Blend (10mg)
Research indicates that peptides CJC-1295 and GHRP-6 may exert potential action on growth hormone release. When presented as a blend, they may possibly induce synergistic action, stimulating an organism’s synthesis and secretion of growth hormones. This peptide blend may possibly help repair mild injuries associated with muscles and surrounding ligaments. GHRP-6 peptide is a synthetic six amino acid peptide analog of ghrelin, a naturally occurring peptide that is considered by scientists to stimulate the secretion of growth hormones and help maintain their concentrations.(1) To do so, researchers hypothesize that it may activate what is known as the growth hormone secretagogue receptor (GHS-R1a). In terms of structure, GHRP-6 does not appear to share any homology with ghrelin despite its affinity to the receptors, but instead it appears to be an opioid analog of the peptide Met-enkephalin. Yet, researchers suggest it lacks the opioid activity which is typically associated with these enkephalins. Thus, GHRP-6 is a synthetic hexapeptide that researchers have classified in the group of growth hormone secretagogues (GHSs). CJC-1295, also referred to as tetra-substituted GRF (1-29), is a synthetic peptide analog of the naturally occurring growth hormone-releasing hormone (GHRH), which is believed by researchers to trigger the release of growth hormones.(2) It is essentially equivalent to the shortest chain of amino acids that may potentially attach to the GHRH receptors, which are the first 29 amino acids of GHRH. The key structural distinctions between CJC-1295 and GRF (1-29) are found in four altered amino acids of the original 29 amino acids of GHRH. These modifications involve the 2nd, 8th, 15th, and 27th amino acids, and may potentially enhance the peptide's resistance to degradation by the enzyme dipeptidyl peptidase-4. Specifically, the modifications include: The substitution of L-alanine with D-alanine at the 2nd position which is believed to increase resistance to molecular breakdown. Replacing asparagine with glutamine at the 8th position which may potentially reduce asparagine rearrangement and amide hydrolysis. The replacement of glycine with alanine at the 15th position which is hypothesized to augment bioactivity. Changing methionine with leucine at the 27th position which is posited to inhibit methionine oxidation. Chemical Makeup(2)(3) Molecular Formula: CJC-1295 peptide: C152H252N44O42 GHRP-6 peptide: C46H56N12O6 Molecular Weight: CJC-1295 peptide: 3367.9 g/mol GHRP-6 peptide: 873.0 g/mol Other Known Titles: Growth hormone-releasing hexapeptide CJC-1295 with DAC CJC-1295 without DAC Both forms of the CJC-1295 peptide essentially exert the same action; however, the addition of DAC (known as the drug affinity complex) appears to change the duration of the action of the peptide. CJC-1295 with DAC may have a longer-lasting action than CJC-1295 without DAC. This could be attributed to the proposed ability of the DAC to attach itself to proteins in the plasma. Specifically, the DAC element involves the connection of a lysine derivative, namely N-epsilon-3-maleimidopropionamide, to the C terminus of CJC-1295. The fusion of this altered amino acid sequence with the DAC element may possibly boost the pharmacokinetics of CJC-1295, prolonging its coexistence with plasma proteins to roughly 8 days, while concurrently preserving a noticeable affinity towards GHRH receptors, akin to the affinity demonstrated by CJC-1295 without DAC. Research and Clinical Studies CJC-1295 & GHRP-6 Peptide Blend and Growth Hormone Levels A clinical trial(4) was conducted in male test subjects aged between 20 and 40. All subjects were divided into two groups; one was presented with a placebo, and the rest received the CJC-1295 peptide. A blood sample was collected from all the subjects before and after peptide presence. Based on these samples, researchers reported that the peptide possibly contributed to a 7.5-fold increase in the subjects’ growth hormone levels compared to the placebo group. The growth hormone levels appeared to increase gradually and remained unchanged one week after the peptide presence. In another clinical study,(5) the peptide was given in ascending concentrations in a group of test subjects aged between 20 and 60. All subjects were divided into two groups – one was presented with the peptide, while the other with a placebo. After the end of the study, when blood samples were examined, it was noted that there appeared to be concentration-dependent action, up to 10-fold, in the levels of the subjects’ growth hormones. As per Madalina Ionescu, et al., “The marked enhancement of trough GH levels by continuous GHRH stimulation implicates the importance of this effect on increasing IGF-I. Long-acting GHRH preparations may benefit patients with intact pituitary GH secretory capability.” IGF-1 stands for insulin-like growth factor-1. It is considered by researchers to be the main anabolic mediator of growth hormone. In a clinical study focusing on the GHRP-6 peptide,(6) younger test subjects between 6 and 11 were presented with the peptide. Some were only given the peptide, while the rest were presented with a blend of peptide and arginine (a growth hormone booster). After the completion of the study, it was reported by the researchers that the growth hormone levels appeared to have increased exponentially and in equal concentrations in all subjects, seemingly regardless of the presence of arginine. CJC-1295 & GHRP-6 Peptide Blend and Hypothyroidism Hypothyroidism is characterized by low levels of growth hormones in an organism. In a 1997 clinical study,(7) subjects with hypothyroidism were presented with either GHRP-6 peptide, GHRH peptide, or a blend of peptides (such as CJC-1295) and GHRP-6. Post-study, it was reported that subjects presented with the blend exhibited apparently significantly higher levels of growth hormones than the individual peptides alone. The GHRP-6 peptide is considered to be an antagonist of somatostatin, which may be an inhibitor of growth hormone secretion. Due to this, the peptide blend appeared to yield a higher result. As per F R Pimentel-Filho et al., “When GHRP-6 was associated with GHRH, a significant increase in the GH response was observed in these patients, which could suggest a role for somatostatin in this process. Our data suggest that thyroid hormones modulate GH release induced by GHRH and GHRP-6 through different mechanisms. However, additional studies are necessary to elucidate this hypothesis further.” CJC-1295 and GHRP-6 Peptide Blend and Cellular Repair Experimental animal models were induced with injury and multiple organ failure. They were then presented with either the GHRP-6 peptide or a combination of GHRP-6 and epidermal growth factor (EGF). Based on the laboratory results, it was observed that the peptide might affect the gut epithelial cells of these animal subjects, as well as possibly increasing cellular migration at three times the usual rate. In addition, it appeared to reduce any adverse action of such failure by 50-85%.(8) GHRP-6 might also show a preference for CD36 receptors, potentially found on the surface of many cell types, such as fat cells, muscle cells, and immune cells. These receptors could have various potential functions, such as participating in fat metabolism, acting as a collector receptor for fats, aiding their absorption, and maybe influencing immune reactions and inflammation. The pathways of CD36 might also have a part in regulating the formation of new blood vessels. By potentially affecting inflammation and angiogenesis, GHRP-6 may further help improve cellular repair in various tissues. CJC-1295 and GHRP-6 Peptide Blend and Diabetes-Induced Gastrointestinal Activity Diabetes is considered by scientists to significantly impact the gastrointestinal system and may reduce the gastric emptying rate and colonic and intestinal transit. Research(9) conducted on experimental mouse models induced with diabetes were subjected to growth hormone release-stimulating peptides (such as GHRP-6). The peptide presence appeared to increase the rate of gastric emptying and intestinal transit, suggesting the peptide’s action in reversing the impacts induced by diabetes. No change was seen in the colonic transit. As per Zheng Q et al., peptides such as GHRP-6 “[have…] potential […] [for] delayed upper gastrointestinal transit.” CJC-1295 and GHRP-6 Peptide Blend and Heart Rate Preliminary research(10) was conducted in mice that suggested GHRH derivative analogs (such as the CJC-1295 peptide) may have the potential to stabilize heart rate and improve functionality following a heart attack. Andrew V. Schally et al. reported that the peptide appears to promote cardiac tissue repair and improve the blood pump capacity of the heart. The researchers observed that the results “[suggest] that GHRH agonists promote repair of cardiac tissue, improving ejection fraction and reducing infarct size in rats, reducing infarct scar in swine, and attenuating cardiac hypertrophy in mice.” CJC-1295 & GHRP-6 Peptide Blend and Neuroprotection The GHRP-6 peptide may be linked to the protection and repair of nervous tissue. A study examined its potential on the IGF-1 system in the brains of murine models.(11) GH potential actions are typically thought to be channeled through IGF-1, so the research focused on how the brain's IGF-1 system is influenced. It was found that a one-week exposure to GHRP-6 seemed to boost IGF-1 mRNA levels in the hypothalamus, cerebellum, and hippocampus, but not the cerebral cortex. This hints that GH and GHRP-6 may potentially boost IGF-1 expression in certain brain regions. The study also looked into the expression of the IGF receptor and IGFBP-2, an IGF-binding protein, but no significant variations in activity were found after the peptide was introduced. Nonetheless, the phosphorylation of Akt and Bad might have been triggered in regions where IGF-1 levels rose. This suggests that GH and GHRP-6 might activate intracellular pathways related to cell survival in response to growth factors. Bad is part of the Bcl-2 protein family, which plays a crucial role in cell death. In contrast, Akt is a protein kinase involved in various cellular functions like glucose metabolism, apoptosis, cell growth, transcription, and cell movement. No changes were noted in MAPK, another protein kinase, or glycogen synthase kinase-3beta. Additionally, the antiapoptotic protein Bcl-2 was found to be elevated in regions with increased IGF-1, while the proapoptotic protein Bax remained unchanged. This may imply a move towards cell survival and away from apoptosis. Finally, IGFBP-5, which is considered to be part of neuron survival processes, was mainly elevated in the hypothalamus, indicating a possible neuroendocrine function. CJC-1295 and GHRP-6 blend is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References Berlanga-Acosta, Jorge, et al. “Synthetic Growth Hormone-Releasing Peptides (GHRPs): A Historical Appraisal of the Evidences Supporting Their Cytoprotective Effects.” Clinical Medicine Insights. Cardiology vol. 11 1179546817694558. 2 Mar. 2017, doi:10.1177/1179546817694558. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5392015/ National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 91976842, CJC1295 Without DAC. https://pubchem.ncbi.nlm.nih.gov/compound/CJC1295-Without-DAC. National Center for Biotechnology Information (2023). PubChem Compound Summary for CID 9919153, Growth hormone releasing hexapeptide. https://pubchem.ncbi.nlm.nih.gov/compound/9919153. Ionescu M, Frohman LA. Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog. J Clin Endocrinol Metab. 2006 Dec;91(12):4792-7. doi: 10.1210/jc.2006-1702. Epub 2006 Oct 3. PMID: 17018654. https://pubmed.ncbi.nlm.nih.gov/17018654/ Teichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA. 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. J Clin Endocrinol Metab. 2006 Mar;91(3):799-805. doi: 10.1210/jc.2005-1536. Epub 2005 Dec 13. PMID: 16352683. https://pubmed.ncbi.nlm.nih.gov/16352683/ Bellone J, Ghizzoni L, Amaretti G, Volta C, Boghen MF, Bernasconi S, Ghigo E. Growth hormone-releasing effect of oral growth hormone-releasing peptide 6 (GHRP-6) administration in children with short stature. Eur J Endocrinol. 1995 Oct;133(4):425-9. https://pubmed.ncbi.nlm.nih.gov/7581965/ Pimentel-Filho FR, Ramos-Dias JC, Ninno FB, Façanha CF, Liberman B, Lengyel AM. Growth hormone responses to GH-releasing peptide (GHRP-6) in hypothyroidism. Clin Endocrinol (Oxf). 1997 Mar;46(3):295-300. https://pubmed.ncbi.nlm.nih.gov/9156038/ Cibrián D, Ajamieh H, Berlanga J, León OS, Alba JS, Kim MJ, Marchbank T, Boyle JJ, Freyre F, Garcia Del Barco D, Lopez-Saura P, Guillen G, Ghosh S, Goodlad RA, Playford RJ. Use of growth-hormone-releasing peptide-6 (GHRP-6) for the prevention of multiple organ failure. Clin Sci (Lond). 2006 May;110(5):563-73. https://pubmed.ncbi.nlm.nih.gov/16417467/ Zheng, Q., Qiu, W. C., Yan, J., Wang, W. G., Yu, S., Wang, Z. G., & Ai, K. X. (2008). Prokinetic effects of a ghrelin receptor agonist GHRP-6 in diabetic mice. World journal of gastroenterology, 14(30), 4795–4799. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2739343/ Schally AV, Zhang X, Cai R, Hare JM, Granata R, Bartoli M. Actions and Potential Therapeutic Applications of Growth Hormone-Releasing Hormone Agonists. Endocrinology. 2019 Jul 1;160(7):1600-1612. doi: 10.1210/en.2019-00111. PMID: 31070727. Frago LM, Pañeda C, Dickson SL, Hewson AK, Argente J, Chowen JA. Growth hormone (GH) and GH-releasing peptide-6 increase brain insulin-like growth factor-I expression and activate intracellular signaling pathways involved in neuroprotection. Endocrinology. 2002 Oct;143(10):4113-22. doi: 10.1210/en.2002-220261. PMID: 12239123. 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.
AHK-Cu (200mg)
AHK-Cu is a peptide composed of amino acids alanine, histidine, and lysine, with a copper ion coordinated by various parts of these three amino acids.(1) This peptide appears to be naturally present in the bloodstream and has been suggested as a potential element in regulating the growth, development, and apoptosis of vascular endothelial cells. AHK-Cu, also known as copper AHK, has been researched for its potential in hair growth and supporting skin tissue integrity. This peptide has been suggested to exhibit its potential primarily on fibroblasts, responsible for maintaining and growing the extracellular matrix (ECM) components surrounding the cells. Fibroblasts also appear to secrete various biological substances, including the Vascular Endothelial Growth Factor (VEGF), which is suggested to promote the formation of new blood vessels. The copper ion in AHK-Cu is suggested to be involved in enzyme activity related to collagen and elastin synthesis. These two proteins are critical components of the extracellular matrix and play a role in maintaining the skin tissues' structural integrity. Copper ions are also suggested to exhibit antioxidant properties. Chemical Makeup(2) Molecular Formula: C15H25CuN6O4 Molecular Weight: 416.9 g/mol Other known titles: ALA-HIS-LYS-CU, L-Alanyl-κN-L-histidyl-κN,κN3-L-lysinato(2-)]copper Monohydrochloride Research and Clinical Studies AHK-Cu Peptide and Antioxidative Potential AHK-Cu is posited to have potent antioxidant qualities, primarily due to its distinct amino acid structure. Based on the antioxidative properties of this peptide, studies have suggested its potential in amplifying hair follicle size, which may increase growth. This peptide has been the focus of numerous in-vitro investigations, particularly concerning its role in hair growth. These studies uniformly suggest AHK-Cu's potential to foster hair follicle development. In addition to hair growth, AHK-Cu's scope of application may extend to cell aging, wound healing, and other areas, according to researchers. They posit its potential role in boosting dermal cell multiplication and survival, both of which are essential in collagen production. Collagen is a vital element for maintaining skin cell turnover and function, and the increased cell activity provided by AHK-Cu may facilitate this process.(3) AHK-Cu Peptide and Hair Follicle Development Researchers posit that the tripeptide AHK-Cu may potentially stimulate the proliferation of dermal fibroblasts, a type of cell that produces substances like vascular endothelial growth factor (VEGF), which are considered to be crucial for the growth of blood vessels. AHK-Cu may also reduce the secretion of transforming growth factor-beta1 by dermal fibroblasts. In a recent study,(4) the potential of AHK-Cu on hair growth was investigated. It was suggested that the peptide may promote the elongation of hair follicles and the proliferation of dermal papilla cells (DPCs), which are specialized fibroblasts with a potential to increase the growth and development of hair follicles. Moreover, the authors suggested that the presence of AHK-Cu may have reduced the number of apoptotic dermal papilla cells. Further analysis suggested that the peptide may have increased the ratio of Bcl-2/Bax, and potentially decreased cleaved caspase-3 and PARP levels, two markers of cell death. The Bcl-2/Bax ratio is suggested to play a potential role in the regulation of apoptosis. Bcl-2 is posited as an anti-apoptotic protein that apparently inhibits cell death, while Bax is suggested to be a pro-apoptotic protein that promotes cell death. Thus, a higher Bcl-2/Bax ratio is posted as a predominance of Bcl-2, which may inhibit apoptosis and apparently promotes cell survival. Ultimately, the researchers suggested that AHK-Cu “stimulated the elongation of […] hair follicles […] and the proliferation of DPCs in vitro.” Based on these observations, the researchers commented, “The present study proposed that AHK-Cu promotes the growth of [...] hair follicles, and this stimulatory effect may occur due to stimulation of the proliferation and the preclusion of the apoptosis of DPCs.”(4). Other researchers delving into this trial also noticed that the peptide may have interacted with VEGF and Transforming Growth Factor Beta 1 (TGF-β1). TGF-β1 is researched for its role in cell proliferation, differentiation, and apoptosis. It is posited to be involved in several cellular processes, including the regulation of immune responses and wound healing. By potentially downregulating TGF-β1, AHK-Cu may alter these cellular processes, possibly affecting cell growth and the immune response at a cellular level. On the other hand VEGF is researched for its role in angiogenesis, the formation of new blood vessels from pre-existing vessels. The upregulation of VEGF by AHK-Cu might imply an enhanced potential for angiogenesis, which could influence nutrient and oxygen supply at the cellular level.(5) VEGF specifically is posited to foster the development of blood vessels surrounding hair follicles. This action potentially aids in delivering nutrients and oxygen to the hair follicles, thereby supporting hair growth. AHK-Cu Peptide and Alopecia Research The study examined the potential of two formulations containing growth factors and peptides such as vascular endothelial growth factor, basic fibroblast growth factor, insulin-like growth factor-1, keratinocyte growth factor, and copper tripeptide 1 and related peptides such as AHK-Cu, suspended in a sterile vehicle. The experiment investigated the potential cytotoxicity of these factors using in vitro keratinocyte and fibroblast cell assays. The formulations were also investigated for their potential for hair growth and hair follicle viability in cases of secondary alopecia.(1) The authors suggested that both formulations appeared to produce a positive response regarding hair growth in the animals. The formulations also were posited to be impactful when tested alongside agents that may be associated with alopecia. Researchers Rinky Kapoor et al. state, “Results seem encouraging enough to warrant a trial in [...] secondary alopecia.” (1) AHK-Cu Peptide and Skin Tissue Integrity Preliminary lab studies have suggested that the core molecule of the peptide, AHK, may stimulate the growth of fibroblast cells and the production of collagen. Notably, AHK appears to improve the survival and multiplication of dermal fibroblasts, which are researched for their potential for generating vital skin proteins like collagen. In experiments with normal dermal fibroblasts, AHK was observed to apparently boost both cell growth and viability, alongside enhancing collagen type I production. This conclusion was drawn by measuring collagen type I levels produced by fibroblasts in a cell culture following exposure to varying concentrations of AHK. The studies indicated that AHK's presence may have raised collagen type I production, with a threefold increase compared to the control group. These results imply that AHK could potentially rejuvenate the extracellular matrix and contribute to skin function.(6) AHK-Cu peptide is available for research and laboratory purposes only. Please review and adhere to our Terms and Conditions before ordering. References Kapoor R, Shome D, Vadera S, Kumar V, Ram MS. QR678 & QR678 Neo Hair Growth Formulations: A Cellular Toxicity & Animal Efficacy Study. Plast Reconstr Surg Glob Open. 2020 Aug 25;8(8):e2843. doi: 10.1097/GOX.0000000000002843. PMID: 32983753; PMCID: PMC7489598. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7489598/ AHK-Cu, ChemBK. https://www.chembk.com/en/chem/AHK-Cu Kecel-Gunduza, S., Kocb, E., Bicaka, B., Kokcub, Y., Ozela, A. E., & Akyuzc, S. (2020). IN SILICO ANALYSIS FOR CHARACTERIZING THE STRUCTURE AND BINDING PROPERTIES OF ALA-HIS-LYS (AHK) TRIPEPTIDE. The Online Journal of Science and Technology-July, 10(3). Pyo HK, Yoo HG, Won CH, Lee SH, Kang YJ, Eun HC, Cho KH, Kim KH. The effect of tripeptide-copper complex on human hair growth in vitro. Arch Pharm Res. 2007 Jul;30(7):834-9. doi: 10.1007/BF02978833. PMID: 17703734. https://pubmed.ncbi.nlm.nih.gov/17703734/ Sadgrove NJ, Simmonds MSJ. Topical and nutricosmetic products for healthy hair and dermal anti-aging using "dual-acting" (2 for 1) plant-based peptides, hormones, and cannabinoids. FASEB Bioadv. 2021 Jun 6;3(8):601-610. doi: 10.1096/fba.2021-00022. PMID: 34377956; PMCID: PMC8332470. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8332470/ Patt, L. M., & Procyte, A. (2009). Neova® DNA Repair Factor Nourishing Lotion Stimulates Collagen and Speeds Natural Repair Process. skin, 1, 2. 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.