Tripeptide-29: Potential Properties

One of collagen’s building blocks, Tripeptide-29, is a synthetic protein. The amino acid sequence of collagen repeats every three amino acids throughout the polymer chain. These iterations combine to produce a secondary structure, which generates tertiary and even quaternary structures. Compared to peptide subunits, these complex structures may exhibit various emergent features. However, modifications to peptide building blocks may have an effect. The most common structure for quaternary collagen compounds and subunits is Gly-Pro-X, Gly-Xo-X, or Gly-X-Hyp. GlyPro Hyp peptides like Tripeptide-29 are full synthetic analogs of naturally occurring collagen-building components.

Studies suggest that collagen may not function properly without Tripeptide-29. Their amino acid sequence and relative frequency may affect collagen molecules’ tertiary and quaternary characteristics. Collagen is a structural protein that can aid cell adhesion, tissue control, and wound healing. As a result, Tripeptide-29 may have an impact on a variety of linked physiological features.

Tripeptide-29 Research

As suggested by in vitro research, the unpolymerized version of Tripeptide-29 may act as a partial agonist of the GPVI collagen receptor. “The monomeric compounds partly inhibit the release of [3H]5-HT by CRP,” the researchers write, “suggesting that they are semi-agonists of the collagen receptor GPVI.” Platelets have GPVI expressed on their surface. Platelets, which resemble cells, play an early role in clotting blood. In vascular tissue, GPVI receptors initiate blood clot formation and tissue healing by activating platelet aggregation in response to collagen. Therefore, collagen fibers are widely believed to be thrombus-forming. Thrombus development may occur due to collagen thrombus formation when control is disrupted. Tripeptide-29 cross-linking seems to stimulate GPVI activation, which might provide light on how this peptide establishes an “accurate” coagulation environment in a range of bleeding and clotting problems.

Tripeptide-29 and Collagen

Preliminary research suggests that short peptides like Tripeptide-29 may be able to modulate collagen stability. In particular, investigations of Tripeptide-29 have led researchers to speculate that the last peptide of the tripeptide monomer seems to have the most impact on the final collagen structure. The peptide at position C impacts collagen stability the most for ABC monomers. Scientists hope to one day use this research to create artificial implants that mimic natural tissues like bone, cartilage, and teeth.

Tripeptide-29 and Free Radicals

Free radical damage is an important factor in the aging of cells and tissues. The efficiency of umerous natural defenses diminish with time, leaving the organism vulnerable to free radical damage. Collagen monomers, including Tripeptide-29, found in collagen hydrolysates, may be potent radical scavengers, as suggested by research on Namako. The potential of tripeptide monomers to scavenge radicals may depend on their structure. Although Tripeptide-29 hasn’t been studied, scientists are interested in learning more about how peptides like it may be employed in nutrition. Scientists theorized that “collagen hydrolysates from S. vastus may be utilized as a functional component in food and nutraceutical products.”

Tripeptide-29 and Tissue Fibrosis

Tripeptide-29 has been suggested to suppress dipeptidyl peptidase IV activity in in vitro tests of pigskin, cow skin, fish scales, and chicken feet. Immune-infected cells are rich in dipeptidyl peptidase IV (DPP4). It is a necessary component of the cell membrane that degrades growth factors, chemokines, neuropeptides, and vasoactive peptides without regard to their specific targets. In addition, it degrades incretin, a hormone that raises blood sugar, playing a crucial role in glucose metabolism. Animal studies have suggested that DPP4 has a role in producing fibrosis in organs such as the kidneys and liver via suppression of the enzyme, which inhibits scarring during the illness that affects these organs. Since diabetes is the most common cause of renal fibrosis, Tripeptide-29 may have a dual purpose here. Inhibiting dipeptidyl peptidase 4 (DPP4), as Tripeptide-29 may do, increases glucose availability for use by cells and decreases fibrosis, paving the door for further research into the potential management of diabetes and its severe consequences.

Tripeptide-29 and Skin

Tripeptide-29 for sale, along with other tripeptides, has attracted scientific attention for its potential to minimize external symptoms of age-related decline. Animal studies suggest that enhancing contours, minimizing skin deformation, and boosting moisture by tripeptides may reduce visible symptoms. Research also suggests that tripeptides might help diminish the visibility of brown and red patches and soften the skin’s texture. Investigations propose that 90% of research models in a single study appeared to experience an improvement in skin elasticity and moisture. Scientists have hypothesized that Tripeptide-29, combined with certain hexapeptides, may stimulate skin regeneration and reduce wrinkle depth and formation. About half of the animals in these experiments seemed to exhibit better skin appearance after receiving peptide paste twice daily.

References

[i] Asselin J, Knight CG, Farndale RW, Barnes MJ, Watson SP. Monomeric (glycine-proline-hydroxyproline)10 repeat sequence is a partial agonist of the platelet collagen receptor glycoprotein VI. Biochem J. 1999 Apr 15;339 ( Pt 2)(Pt 2):413-8. PMID: 10191274; PMCID: PMC1220172.

[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] Abedin MZ, Karim AA, Latiff AA, Gan CY, Ghazali FC, Barzideh Z, Ferdosh S, Akanda MJ, Zzaman W, Karim MR, Sarker MZ. Biochemical and radical-scavenging properties of sea cucumber (Stichopus vastus) collagen hydrolysates. Nat Prod Res. 2014;28(16):1302-5. doi: 10.1080/14786419.2014.900617. Epub 2014 Mar 27. PMID: 24670209.

[iv] Hatanaka T, Kawakami K, Uraji M. Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity. J Enzyme Inhib Med Chem. 2014 Dec;29(6):823-8. doi: 10.3109/14756366.2013.858143. Epub 2014 Mar 20. PMID: 24650211.

[v] Min HS, Kim JE, Lee MH, Song HK, Kang YS, Lee MJ, Lee JE, Kim HW, Cha JJ, Chung YY, Hyun YY, Han JY, Cha DR. Dipeptidyl peptidase IV inhibitor protects against renal interstitial fibrosis in a mouse model of ureteral obstruction. Lab Invest. 2014 Jun;94(6):598-607. doi: 10.1038/labinvest.2014.50. Epub 2014 Mar 31. PMID: 24687121.