Syn-Coll, also known as Palmitoyl Tripeptide-5, is a synthetic lipopeptide composed of a tripeptide chain — lysine, valine, and lysine — attached to a palmitoyl (fatty acid) group, which helps enhance its stability and absorption in tissue environments. It belongs to the class of matrikine-mimicking peptides, meaning it is designed to mimic small protein fragments that naturally occur when the extracellular matrix breaks down and signal the body to initiate structural protein production. The palmitoyl modification places it in the same broad family as other fatty acid-conjugated peptides that have attracted interest in dermatological and tissue research contexts. With the molecular formula C33H65N5O5 and a molecular weight of approximately 611.9 g/mol, Syn-Coll is studied in laboratory settings to better understand how synthetic peptide signals may interact with connective tissue biology at a cellular level. It is intended strictly for research purposes and is not approved for human consumption or therapeutic use.
| CAS Number | 623172-55-4 |
| Molecular Formula | C33H65N5O5 |
| Molecular Weight | 611.90 g/mol |
| IUPAC Name | (2S)-6-amino-2-[[(2S)-2-[[(2S)-6-amino-2-(hexadecanoylamino)hexanoyl]amino]-3-methylbutanoyl]amino]hexanoic acid |
| PubChem CID | 11950477 |
Syn-Coll is a synthetic peptide that researchers have studied primarily in the context of skin biology, with particular interest in its potential effects on collagen synthesis and extracellular matrix remodeling. Studies have examined this compound in relation to fibroblast activity, as fibroblasts are the primary cells responsible for producing structural proteins such as collagen types I and III in connective tissue. In vitro investigations have explored how Syn-Coll may interact with cellular signaling pathways involved in dermal matrix maintenance and the regulation of matrix metalloproteinases, which are enzymes that contribute to collagen degradation. Research has also investigated its molecular mimicry of endogenous peptide sequences, as its design is based on structural motifs associated with naturally occurring collagen-stimulating signals. Published research specifically on Syn-Coll as an isolated compound remains limited, and much of the available scientific context comes from broader studies on synthetic collagen-stimulating peptides and cosmetic ingredient research rather than formal peer-reviewed biomedical trials.
No published research abstracts are currently available for this compound in our database.