Tripeptide-29 And Collagen Peptide Research
Tripeptide-29 is a peptide comprised of the amino acids glycine, proline, and hydroxyproline.
It is also known as a collagen peptide because it is a naturally occurring peptide in animal collagen.
Research on animals suggests that Tripeptide 29 may enhance skin texture, decrease the appearance of fine lines and wrinkles, and rehydrate dry patches.
Experts are currently studying the potential of Tripeptide on the skin. If you need to buy collagen peptides for research, navigate to the Biotech Peptides website. To learn more about this peptide, keep reading.
Tripeptide-29: What is it?
Studies suggest that Tripeptide-29 is a synthetic peptide that is an important structural component of collagen.
An animal’s connective tissues, including its hair, nails, skin, tendons, ligaments, and bones, rely on collagen, an abundant protein.
The structural units of this long-chain polymer include glycine, proline, and hydroxyproline. A crucial component of type 1 collagen is the Gly-Pro-Hyp peptide Tripeptide-29.
Collagen is a lengthy sequence of amino acids, as we can see with additional investigation.
Upon dismantling this structure, peptides composed of sequences of amino acids are produced. Research suggests that to replenish lost collagen, the skin may take instructions from these peptides.
Doing so may stimulate endogenous collagen production.
It has been hypothesized that Tripeptide-29 may alter collagen tertiary and quaternary structures.
As purported by animal research, collagen is a structural protein that may help wound healing, cell adhesion, and tissue regulation.
What Is Collagen Type 1?
One of the most prevalent forms of protein in animals is collagen type 1, which contains tripeptides.
The connective tissue component collagen 1 has been suggested in animal studies to promote and sustain many biological factors, most of which is the extracellular matrix of skin.
Findings imply this peptide may be useful in the context of strengthening bones, ligaments, and muscles in animal research models.
Tripeptide-29 and Free Radicals
Investigations purport that tripeptides may have several potential uses in skin studies, and we’ll go over them all here.
These studies propose that preventing free radical damage to animals may be one of its primary research applications.
Free radical damage is the primary cause of the gradual destruction of cells and tissues. Several defenses work together to keep free radicals at bay, but over time, these defenses start to fail.
Research using sea cucumbers has purported that collagen hydrolysates containing monomers like Tripeptide-29 may be superior radical scavengers.
By scavenging free radicals, animal research postulates that Tripeptide may help keep skin, hair, nails, bones, organs, and tendons functional.
Research on animals suggests that this collagen peptide may improve skin quality while keeping the animal cells functioning at a high level over a prolonged period of time.
Maybe the characteristics of this peptide may be better understood with more research.
Tripeptide-29 and Skin
Tripeptide-29 may also have skin anti-aging properties, as proposed by recent animal research. Specialists speculate that a topical tripeptide solution may enhance skin hydration and structure while slowing down the deformation of aging skin.
Additional studies hint that tripeptides might have the potential to enhance skin tone and smooth skin texture and reduce the appearance of redness, brown spots, and other skin discolorations in animals.
Fascinatingly, the skin of up to 90% of the animals in the research appeared to become more elastic, flexible and hydrated.
Animal studies have indicated that Tripeptide-29 when given topically with certain hexapeptides, could reduce the appearance of wrinkles and fine creases along the skin surface.
A significant improvement in skin tone was speculated in around 50% of the mice given the peptide.
Tripeptide-29 and Cellular Fibrosis
Studies on animals have suggested that Tripeptide-29 may decrease the activity of dipeptidyl peptidase-IV. One of the most important enzymes in cell death and immunological signaling is dipeptidyl peptidase IV or DPP4.
In several animal experiments, its capacity to degrade growth factors, neuropeptides, chemokines, and vasoactive peptides suggested its crucial role in cell membranes.
Furthermore, animal studies have hinted that Tripeptide-29 collagen peptide may have the potential to improve glucose metabolism and lower blood glucose levels.
Supplemental animal research indicates that DPP4 may contribute to fibrosis in several organs, including the kidney and liver.
Therefore, reducing organ scarring caused by illness could be achieved by inhibiting this enzyme.
Conclusion
Findings imply that Tripeptide-29 may partially agonize the platelet-expressed collagen receptor GPVI.
Regarding tissue healing and clot formation in animals, this receptor is assumed to be crucial for initiating platelet aggregation in vascular tissue, a collagen-mediated process.
This is why collagen fibers are considered thrombogenic by researchers.
There are encouraging speculations that Tripeptide 29 might be a useful peptide for various concerns; however, the research is still in its early stages. Scientists are curious about this collagen peptide’s potential in widespread research areas.
Tripeptide-29 is not accessible for personal use but only for scientific study.
Please note that none of the substances mentioned in this article have been approved for human use.
References
[i] Wiśniewski, K., Artemowicz, B., Lutostańska, A., Maćkowiak, J., & Koziołkiewicz, W. (1994). Central activity of peptide Gly-Pro-Hyp–the main component of collagen degradation products mixture. Acta neurobiologiae experimentalis, 54(1), 33–38.
[ii] Jariashvili, K., Madhan, B., Brodsky, B., Kuchava, A., Namicheishvili, L., & Metreveli, N. (2012). UV damage of collagen: insights from model collagen peptides. Biopolymers, 97(3), 189–198. https://doi.org/10.1002/bip.21725
[iii] J. Asselin, C. G. Knight, R. W. Farndale, M. J. Barnes, and S. P. Watson, “Monomeric (glycine[1]proline-hydroxyproline)10 repeat sequence is a partial agonist of the platelet collagen receptor glycoprotein VI,” Biochem. J., vol. 339 ( Pt 2), pp. 413–418, Apr. 1999.
[iv] K. Mizuno, D. H. Peyton, T. Hayashi, J. Engel, and H. P. Bächinger, “Effect of the -Gly-3(S)- hydroxyprolyl-4(R)-hydroxyprolyl- tripeptide unit on the stability of collagen model peptides,” FEBS J., vol. 275, no. 23, pp. 5830–5840, Dec. 2008.
[v] M. Z. Abedin et al., “Biochemical and radical-scavenging properties of sea cucumber (Stichopus vastus) collagen hydrolysates,” Nat. Prod. Res., vol. 28, no. 16, pp. 1302–1305, 2014.
[vi] T. Hatanaka, K. Kawakami, and M. Uraji, “Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity,” J. Enzyme Inhib. Med. Chem., vol. 29, no. 6, pp. 823–828, Dec. 2014.
[vii] H. S. Min et al., “Dipeptidyl peptidase IV inhibitor protects against renal interstitial fibrosis in a mouse model of ureteral obstruction,” Lab. Investig. J. Tech. Methods Pathol., vol. 94, no. 6, pp. 598–607, Jun. 2014.
[viii] A. Garre, G. Martinez-Masana, J. Piquero-Casals, and C. Granger, “Redefining face contour with a novel anti-aging cosmetic product: an open-label, prospective clinical study,” Clin. Cosmet. Investig. Dermatol., vol. 10, pp. 473–482, 2017.
