*One collagen backbone has a synthetic analog in Tripeptide-29. As a long-chain polymer, collagen typically consists of sequences of three amino acids linked in short monomeric repeats. The secondary structures formed by these repeat links and tertiary and even quaternary structures can be assembled from there. There are a lot of emergent features in these complicated structures that the peptide subunits lack.
The final characteristics of a quaternary collage compound can be altered by altering the nature of the peptide subunits. The Gly-Pro-X or Gly-X-Hyp sequence is nearly universal among collagen subunits. Tripeptide-29 is an ideal synthetic substitute for typical collagen components since it is a Gly-Pro-Hyp peptide.
Chemical Formula: C12H19N3O5
Molecular Weight: 285.3 g/mol MoS
Chain of Amino Acids: Gly-Pro-Hyp
Tripeptide-29: What is it?
Tripeptide-29 is an artificial version of a collagen component. Collagen subunits often take the Gly-Pro-X/Gly-X-Hyp structure, which the three-amino-acid long peptide attempts to imitate.
Tripeptide-29 is one of the primary components of bigger molecules of collagen. Studies suggest that this may allow it to alter a collagen molecule’s quaternary and tertiary characteristics depending on its amino acid link and the frequency of the collagen superstructure.
Remember that collagen involves more than just structure; it may also affect cell adhesion, tissue control, and repair. This suggests that Tripeptide-29 may affect many different physiological parameters.
Collagen Properties
It should be noted that collagen is among the most pervasive compounds found in animals. Collagen has a function in the anatomy of ligaments and tendons, walls of blood vessels, the eye’s cornea, dentin, bone, and muscle fibers, development of scars, ocular vitreous humor, the structure of the placenta, spinal cord, integrins, fibronectin, and other transmembrane proteins, as well as cell signaling.
Tripeptide-29 Research
The non-polymerized version of Tripeptide-29 is a partial agonist of the collagen receptor GPVI, according to in vitro studies. Platelets are cell-like entities that express GPVI on their surface. They are responsible for the early generation of blood clots. Collagen activates platelet aggregation in vascular tissue, an essential initial step in clot formation and tissue repair; the GPVI receptor is an essential cog in this wheel. Therefore, collagen fibers are thought to be thrombogenic in general.
Blood clots can form when collagen thrombogenesis is not properly controlled. Tripeptide-29 crosslinking seems to enhance GPVI activation, which raises the possibility that this peptide could provide light on establishing a “just-right” clotting environment in the context of different bleeding/clotting problems.
Tripeptide-29 and Collagen
Short peptides, such as Tripeptide-29, have been the subject of benchtop research into collagen stability modulation. For instance, Tripeptide-29 has been hypothesized to aid in understanding how the final peptide in a tripeptide monomer affects the collagen structure. The peptide at position C in an A-B-C monomer is the most important for the final stability of the collagen. Scientists may be able to use this discovery to develop synthetic implants for various tissues, including teeth, bone, cartilage, and more.
Tripeptide-29 and Free Radical Damage
Cellular and tissue aging are mainly caused by free radical damage. Many mechanisms in the body try to ward off free radical damage, but they all wear out with time. According to sea cucumber research, collagen hydrolysates from monomers such as Tripeptide-29 may be powerful radical scavengers. According to the same study, the structure of the monomer seems to influence scavenger activity.
Tripeptide-29 and Tissue Fibrosis
Investigations purport that Tripeptide-29 may inhibit dipeptidyl peptidase-IV activity, as suggested by in vitro investigations of pig skin, cattle skin, fish scales, and chick feet. Cells involved in immunological signaling and cell death primarily contain the enzyme dipeptidylpeptidase-IV (DPP4). It can degrade chemokines, neuropeptides, growth factors, and vasoactive peptides without bias because it is an integral component of cell membranes. Decomposing incretins, which are hormones that promote a drop in blood glucose levels, also have a significant impact on glucose metabolism.
Research on animals has indicated that DPP4 is involved in the evolution of fibrosis in various organs, including the liver and kidneys. By blocking the enzyme’s activity, scarring caused by diseases of these organs can be avoided. Findings imply that since diabetes is a leading cause of kidney fibrosis, Tripeptide-29 may have an added property in this situation. As Tripeptide-29 may inhibit DPP4 to increase glucose absorption and decrease fibrosis, it has been hypothesized to offer several new lines of inquiry into managing diabetes and its pathologic complications.
Tripeptide-29 and Skin Cells
The possible function of Tripeptide-29 and similar tripeptides in mitigating the aging cycle in skin cells has recently attracted attention amongst researchers. Tripeptides, according to animal studies, may impact structure, texture, and moisture retention, all of which may contribute to the visible impacts of skin cell aging. Additionally, tripeptides have been theorized to diminish the development of patching. Surprisingly, in one study conducted on animal models, 90% reportedly exhibited greater moisture retention and skin structure flexibility due to enhanced elasticity.
Scientists speculate that topical Tripeptide-29, when mixed with specific hexapeptides, may increase skin cell turnover and diminish the depth and development of wrinkles along the skin’s surface.
Buy collagen peptides if you are a researcher interested in further studying the potential of peptides such as Tripeptide-29.
References
[i] J. Asselin, C. G. Knight, R. W. Farndale, M. J. Barnes, and S. P. Watson, “Monomeric (glycine-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.
[ii] 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.
[iii] 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
[iv] 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
[v] 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.
[vi] 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
[vii] A. Reivitis, K. Karimi, C. Griffiths, and A. Banayan, “A single-center, pilot study evaluating a novel TriHex peptide- and botanical-containing eye treatment compared to baseline,” J. Cosmet. Dermatol., vol. 17, no. 3, pp. 467–470, Jun. 2018
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