Home HEALTH Collagen Synthesis Research with Syn-Coll Peptide

Collagen Synthesis Research with Syn-Coll Peptide

Peptides use

Syn-Coll, or Palmitoyl tripeptide-5, is a synthetic peptide molecule. Studies suggest the peptide was created to promote transforming growth factor beta (TGF-), like the natural protein thrombospondin-1 (TSP-1). TGF- is considered a growth factor promoting collagen synthesis, contributing to the maintenance of skin integrity and postnatal skin structure.

TSP-1’s Lys-Arg-Phe-Lys short sequence is suggested to stimulate transforming growth factors. [i] Scientists suggest that Syn-Coll, which contains the Palmitoyl-Lys-Val-Lys, may have a comparable effect on TGF-. Thus, results from cell culture assay with dermal fibroblasts and animal models suggest that it may increase collagen formation in the skin. Syn-Coll has been suggested to stimulate TGF- activity, which may boost Type I and Type III collagen formation by dermal fibroblasts.

Animal models and research have also examined Syn-Coll in-depth, with consistent findings suggesting it may stimulate collagen formation and inhibit its breakdown. Matrix metalloproteinases (MMPs) like MMP1 and MMP3 may be blocked in their tracks by Syn-Coll.

Syn-Coll Peptide and Collagen Synthesis

Studies suggest dermal connective tissue comprises a network of proteins and fibers called the extracellular matrix, and collagen is a key component of this matrix.

Research done recently suggests that Syn-Coll may increase collagen production. Researchers speculate this synthetic peptide may stimulate TGF- production by acting like TSP-1. Syn-Coll may function, in particular, by imitating a segment of TSP-1’s sequence. [ii]

It has been hypothesized that TGF critical growth factor may play a significant role in controlling collagen formation. Researchers speculate Syn-Coll may stimulate cutaneous fibroblasts to produce more type I and type III collagen by activating dormant TGF-. TGF- activation “causes a persistent enhancement in steady-state quantities of type I and type III collagen and fibronectin mRNAs in normal […] dermal fibroblasts,” as suggested by scientists. [iii]

Studies have suggested that compared to Palmitoyl pentapeptide, Syn-Coll may stimulate type 1 collagen production through TGF- to a larger extent. It has been hypothesized by the researchers that “Palmitoyl tripeptide-5, also known as Syn-Coll, may increase collagen 1 production via TGF-b reportedly 60% more effectively than palmitoyl pentapeptide.”

Syn-Coll Peptide and Collagen Degradation

Collagen and other proteins in the extracellular matrix are broken down by matrix metalloproteinases (MMPs). MMPs are important in tissue remodeling and upkeep of the extracellular matrix, and scientists believe they are primarily generated by dermal cells like fibroblasts. However, they postulate that MMPs might contribute to cutaneous collagen degradation when overproduced or dysregulated. Some enzymes, such as matrix metalloproteinase-1 (MMP-1), are thought to break down type I collagen.

Fibroblasts produce MMP-1; conditions including UV radiation, inflammation, and oxidative stress may boost its activity. MMP-3 is another kind of MMP, and it is thought to be able to cleave various proteins found in the extracellular matrix, such as collagens, laminin, fibronectin, proteoglycans, and elastin. Type II collagen, the primary structural component of cartilage, may be a target for its degradative abilities. Type III collagen, which is very prevalent in the skin and blood vessels, has been linked to breakdown by matrix metalloproteinase 3.

Research suggests that Syn-Coll (Palmitoyl tripeptide-5) seems to suppress matrix metalloproteinases that degrade collagen. Researchers also speculate that Syn-Coll (palmitoyl tripeptide-5) may inhibit collagen breakdown by blocking the activities of matrix metalloproteinases 1 and 3. [iv]

Syn-Coll Peptide and Aging

Researchers have suggested that Syn-Coll may significantly reduce the visibility of wrinkles compared to a placebo. They speculated that Syn-Coll (palmitoyl tripeptide-5) might have around 3.5 times the chance to lessen wrinkles’ visibility as the placebo. Presenting Syn-Coll twice daily for 84 days was suggested to be more effective than control groups, placebo, and other peptides at reducing skin roughness and decreasing the appearance of fine lines and wrinkles in one research study examining the impact across 60 test subjects. [v]

Further study is required to comprehensively understand the applications of these compounds within scientific research. The utilization of Syn-Coll peptide is limited to research and educational institutions. corepeptides.com is a reputable platform for researchers to find material. It is important to note that none of the substances discussed in this context have received approval for consumption by either humans or animals, and the use of these compounds outside of laboratory settings is strictly prohibited.


[i] Murphy-Ullrich, J. E., & Poczatek, M. (2000). Activation of latent TGF-beta by thrombospondin-1: mechanisms and physiology. Cytokine & growth factor reviews, 11(1-2), 59–69. https://doi.org/10.1016/s1359-6101(99)00029-5

[ii] Trookman, N. S., Rizer, R. L., Ford, R., Ho, E., & Gotz, V. (2009). Immediate and Long-term Clinical Benefits of a Topical Treatment for Facial Lines and Wrinkles. The Journal of clinical and aesthetic dermatology, 2(3), 38–43.

[iii] Varga, J., Rosenbloom, J., & Jimenez, S. A. (1987). Transforming growth factor beta (TGF beta) causes a persistent increase in steady-state amounts of type I and type III collagen and fibronectin mRNAs in normal human dermal fibroblasts. The Biochemical journal, 247(3), 597–604. https://doi.org/10.1042/bj2470597

[iv] Errante, F., Ledwoń, P., Latajka, R., Rovero, P., & Papini, A. M. (2020). Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Frontiers in chemistry, 8, 572923. https://doi.org/10.3389/fchem.2020.572923

[v] Gorouhi, F., & Maibach, H. I. (2009). Role of topical peptides in preventing or treating aged skin. International journal of cosmetic science, 31(5), 327–345. https://doi.org/10.1111/j.1468-2494.2009.00490.x

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