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Tripeptide-29 200mg

$200 USD
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Product is topical, in powder form, needs reconstitution before use. Please read more on our FAQ page.

Tripeptide-29 is a synthetic peptide which utilizes a three-chain amino acid sequence that mimics one of the basic building blocks of collagen. When speaking of collagen, we should point out that it’s a natural protein found in skin and all internal organs; but it’s not only a structural protein, it also plays a role in cell adhesion, tissue regulation and healing. 

Tripeptide-29, thus, acts as a building block of large collagen molecules and may impact multiple physiological features.

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Description

Tripeptide-29, although small in its structure, is one of the main building blocks for collagen protein. Collagen is an important part of the extracellular matrix, the network of fibers and proteins that make connective tissue. It is responsible for offering support and structure to cellular complexes

Scientists believe that Tripeptide-29 could stimulate collagen synthesis and promote collagen fiber formation. In addition to collagen synthesis, this peptide potentially has other biological functions. For instance, research studies underline its potential as an antioxidant, which might protect cells from damage and oxidative stress. It may also display anti-melanogenic, anti-fibrotic, and anti-inflammatory properties. 

Chemical Structure

  • Molecular Formula: C12H19N3O5
  • Molecular Weight: 285.3 g/mol
  • Other Known Titles: Glycylprolylhydroxyproline

Research and Clinical Studies

Tripeptide-29 and Collagen Stability

Recent research involving short peptides like Tripeptide-29 has shown that they can be used to manage the stability of collagen. Tripeptide-29 has helped researchers understand that the last peptide mainly influences the ultimate collagen structure in a tripeptide monomer. 

In the spectrum of A-B-C, Tripeptide-29 is in the C position, which has the biggest impact on collagen stability. This finding could assist scientists one day in developing synthetic impacts for teeth, bone, cartilage, and more. 

Collagen and Free Radical Damage

Free radicals directly cause tissue and cellular aging. While the body has numerous ways to fight against free radical damage, they all become less effective as we age. Research conducted on sea cucumbers revealed that collagen hydrolysates composed of monomers such as Tripeptide-29 are effective radical scavengers. Even though no research has been carried out on Tripeptide-29, there is an interest in finding out how this peptide could be used in nutraceutical products and food. 

Tripeptide-29 and Tissue Fibrosis 

In vitro clinical studies of chick feet, fish scales, and cattle skin have revealed that Tripeptide-29 is an inhibitor of (DPP4) dipeptidylpeptidase-IV activity. DPP4 is an enzyme mostly found in cells linked to cell apoptosis and immune signaling. 

It is an inseparable part of the cell membrane and indiscriminately destroys vasoactive peptides, neuropeptides, chemokines, and growth factors. DPP4 also plays an important part in glucose metabolism. It breaks down incretins, hormones that minimize blood glucose levels. 

Research on animals showed that DPP4 impacts the development of fibrosis in organs such as the liver and kidneys. Inhibiting the enzyme, therefore, prevents scarring in diseases that affect these organs. Tripeptide-29 might be beneficial in two ways since diabetes causes kidney fibrosis. 

The ability of this peptide to stimulate glucose uptake and minimize fibrosis, both by obstructing DPP4, opens a variety of research opportunities in not only controlling diabetes but its pathologic sequelae as well. 

Tripeptide-29 and Skin Tone 

Scientists recently became interested in the role of Tripeptide-29 and other peptides when it comes to protecting skin against aging. Clinical trials suggest that topical peptides can minimize visible signs of aging by improving hydration, reducing skin deformation, and boosting contour. 

There is also some evidence that indicates that tripeptides can reduce the appearance of red and brown spots and smooth skin texture. In fact, 90% of test subjects which participated in the study showed improved skin moisturization, while increasing elasticity and flexibility. Nearly 50% of subjects appeared to have better skin in all these animal studies. 

Tripeptide-29 and Platelet Aggregation

Collagen-related peptides with a glycine-proline-hydroxyproline pattern are thought to be linked by cysteine residues, which might help increase platelet secretion and clotting through glycoprotein VI receptors.

Researchers think that this receptor is crucial in blood clotting or homeostasis. The Glycoprotein VI receptor is a membrane of the immunoglobulin superfamily of proteins, which is made up of two subunits called alpha and beta. The alpha one is believed to contain a collagen-binding site, while the beta one signals within the platelet. When the glycoprotein VI receptor binds to collagen, it may cause a series of events, leading to the activation of platelets and the formation of a blood clot. 

In animal models, when Tripeptide-29 was applied, it stimulated platelet aggregation and stopped or prevented bleeding. It might boost the formation of thrombi to prevent excessive bleeding.

References:

  • Trzaskalski, N. A., Fadzeyeva, E., & Mulvihill, E. E. (2020). Dipeptidyl Peptidase-4 at the Interface Between Inflammation and Metabolism. *Clinical medicine insights. Endocrinology and diabetes, 13*, 1179551420912972. [https://doi.org/10.1177/1179551420912972](https://doi.org/10.1177/1179551420912972)  
  • Hatanaka, T., Kawakami, K., & Uraji, M. (2014). Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity. *Journal of enzyme inhibition and medicinal chemistry, 29*(6), 823–828. [https://doi.org/10.3109/14756366.2013.858143](https://doi.org/10.3109/14756366.2013.858143)  
  • 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.  
  • Kieffer, T. J., McIntosh, C. H., & Pederson, R. A. (1995). Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. *Endocrinology, 136*(8), 3585–3596. [https://doi.org/10.1210/endo.136.8.7628397](https://doi.org/10.1210/endo.136.8.7628397)  
  • Asselin, J., Knight, C. G., Farndale, R. W., Barnes, M. J., & Watson, S. P. (1999). Monomeric (glycine-proline-hydroxyproline)10 repeat sequence is a partial agonist of the platelet collagen receptor glycoprotein VI. *The Biochemical journal, 339* (Pt 2), 413–418.  
  • Lee, Y. I., Lee, S. G., Jung, I., Suk, J., Lee, M. H., Kim, D. U., & Lee, J. H. (2022). Effect of a Collagen Tripeptide on Antiaging and Inhibition of Glycation of the Skin: A Pilot Study. *International journal of molecular sciences, 23*(3), 1101. [https://doi.org/10.3390/ijms23031101](https://doi.org/10.3390/ijms23031101)  
  • Kasina, S. V. S. K., & Baradhi, K. M. (2022). Dipeptidyl Peptidase IV (DPP IV) Inhibitors. In *StatPearls*. StatPearls Publishing.  
  • Némethy, G., & Scheraga, H. A. (1986). Stabilization of collagen fibrils by hydroxyproline. *Biochemistry, 25*(11), 3184–3188. [https://doi.org/10.1021/bi00359a016](https://doi.org/10.1021/bi00359a016)  
  • 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](https://doi.org/10.1002/bip.21725)  
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