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Tripeptide-29 (topical) (200mg)
Tripeptide-29 peptides are Synthesized and Lyophilized in the USA.
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FREE - 30ml bottle of bacteriostatic water
(Required for reconstitution)
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What is Tripeptide-29?
Tripeptide-29 is a synthesis of one of the basic components of collagen. Collagen is a long-chain polymer composed of short monomer repeats of three consecutive amino acids. These iterations combine to form a secondary structure, which forms tertiary and even quaternary structures. These complex structures have many potential emergent properties not found in peptide subunits. However, changes in the properties of peptide subunits may have an impact. Quaternary collagen compounds and collagen subunits most often follow the pattern of Gly-Pro-X or Gly-Xo-X or Gly-X-Hyp. Tripeptide-29 is a GlyPro Hyp peptide, a complete synthetic analog of common collagen building blocks.
MOLECULAR FORMULA: C12H19N3O5
MOLECULAR WEIGHT: 285.3 g/mol
PUBCHEM: CID 11778669
Tripeptide-29 acts as a component of the larger collagen molecule. Its amino acid sequence and relative frequency may alter collagen molecules’ tertiary and quaternary properties with collagen superstructure. It is important to remember that collagen is a structural protein and plays a role in cell adhesion, tissue regulation, and healing. Therefore, Tripeptide-29 may affect a wide range of related physiological properties.
The Roles of Collagen
Collagen is one of the most ubiquitous molecules in the animal kingdom. It is found in humans, mammals, reptiles, fish, birds, and even algae. Collagen demonstrates its effect in:
– Tendon and ligament structure
– Vascular walls
– Cornea of the eye
– Muscle fibers
– Scar formation
– Vitreous humor of the eye
– Placental structure
– Transmembrane proteins like integrin and fibronectin
– Cell signaling
In vitro studies on Tripeptide-29 posit that the unpolymerized form of the peptide is a partial agonist of the collagen receptor GPVI. The scientists report that “The monomeric peptides partly inhibit the release of [3H]5-HT by CRP, suggesting that they are partial agonists of the collagen receptor GPVI.” GPVI is expressed on the surface of platelets. Platelets are cell-like structures involved in the early formation of blood clots. GPVI receptors play an important role in collagen-induced activation of platelet aggregation in vascular tissue and are the first step toward blood clot formation and tissue repair. Therefore, collagen fibers are generally considered to be thrombus-forming. In the case of dysregulation, collagen thrombus formation can lead to thrombus formation. Interestingly, cross-linking of Tripeptide-29 appears to promote GPVI activation, which may help understand how this peptide creates an “accurate” coagulation environment in a variety of bleeding/ clotting disorders.
Tripeptide-29 and Collagen Stability
Benchtop studies on the role of short peptides such as Tripeptide-29 have shown that they may have the ability to regulate collagen stability. In particular, research studies on Tripeptide-29 have helped scientists understand that the final structure of collagen appears to be primarily affected by the final peptide of the tripeptide monomer. The peptide at position C appears to have the greatest effect on the final collagen stability for ABC monomers. This discovery could help scientists make synthetic implants such as cartilage, bone, and teeth one day.
Tripeptide-29 and Collagen, Free Radical Damage
Free radical damage is a major cause of cell and tissue aging. The body has many defenses against free radical damage, which lose their effectiveness over time. Studies on Namako have shown that collagen hydrolysates composed of monomers, such as Tripeptide-29, may be effective radical scavengers. The structure of tripeptide monomers may affect radical scavenger activity. No studies have been conducted on Tripeptide-29, but there is an appetite among researchers for studying how such peptides can be used in foods and dietary supplements. For example, researchers report that “collagen hydrolysates from S. vastus can be used as a functional ingredient in food and nutraceutical products.”
Tripeptide-29 Regulates Tissue Fibrosis
In vitro studies of pigskin, cow skin, fish scales, and chicken feet have observed that Tripeptide-29 may act as an inhibitor of dipeptidyl peptidase IV activity. Dipeptidyl peptidase IV (DPP4) is primarily found in immune-infected cells. It is an essential part of the cell membrane, which indiscriminately destroys growth factors, chemokines, neuropeptides, and vasoactive peptides. It also plays a major role in glucose metabolism by decomposing incretin, a hormone that stimulates blood sugar levels. Animal studies have suggested that DPP4 plays a role in causing fibrosis in organs such as the kidneys and liver via inhibition of the enzyme, which prevents scarring during the disease that affects these organs. Tripeptide-29 may be doubly useful in this situation, as diabetes is the leading cause of renal fibrosis. The possible ability of Tripeptide-29 to stimulate glucose uptake and reduce fibrosis by inhibiting DPP4 opens the way for many studies to control not only diabetes but also its pathological outcomes.
Tripeptide-29 and Skin Tone
Scientific interest has been generated in the role of Tripeptide-29 and other tripeptides in protecting the skin from normal aging processes. Animal studies suggest that topical application of tripeptides may reduce the visible effects of aging by improving contours, reducing skin deformity, and promoting hydration. Studies further suggest that tripeptides may smooth the texture of the skin and reduce the appearance of brown and red spots. In one particular study, 90% of participants showed improved skin hydration and increased flexibility due to improved elasticity. In combination with certain hexapeptides, topical Tripeptide-29 may promote skin regeneration and reduce fine lines, crow’s feet, bags under the eyes, and eye sockets. Roughly 50% of test animals exhibited improved skin appearance across these studies, where peptide paste was administered twice daily.
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- 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
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Dr. Usman (BSc, MBBS, MaRCP) completed his studies in medicine at the Royal College of Physicians, London. He is an avid researcher with more than 30 publications in internationally recognized peer-reviewed journals. Dr. Usman has worked as a researcher and a medical consultant for reputable pharmaceutical companies such as Johnson & Johnson and Sanofi.