Pal-AHK is a synthetic, lipidated tripeptide derived from the naturally occurring sequence AHK (alanine-histidine-lysine), which is found in human plasma and has been associated with interactions involving copper binding and tissue-related biological processes. The "Pal" prefix refers to palmitoyl, a 16-carbon fatty acid chain that has been chemically attached to the peptide to enhance its stability and ability to interact with lipid-rich environments such as cell membranes. This modification places Pal-AHK in the broader category of palmitoyl peptides, a group that has attracted interest in biochemical and cosmetic research contexts due to the way lipid conjugation can influence peptide behavior at a molecular level. Like its parent sequence, Pal-AHK is studied in research settings for its potential interactions with copper ions and related biological pathways, though all investigations involving this compound are conducted strictly for laboratory and research purposes only and it is not intended for human use.
| Molecular Formula | C30H54N6O5 |
| Molecular Weight | 578.80 g/mol |
| IUPAC Name | 6-amino-2-[[2-[[2-(hexadecanoylamino)acetyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]hexanoic acid |
| PubChem CID | 66927173 |
Pal-AHK is a palmitoylated tripeptide composed of alanine, histidine, and lysine, and researchers have primarily studied it in the context of skin biology and dermal tissue remodeling. In vitro studies have examined its potential role in stimulating fibroblast activity and extracellular matrix protein synthesis, particularly in relation to collagen and structural proteins that contribute to skin architecture. Research has also investigated how palmitoylation of short peptide sequences like AHK may influence cellular uptake and interaction with dermal cells, as the fatty acid moiety is thought to facilitate penetration through lipid-rich barriers. Some studies have explored copper-binding tripeptides with similar structural motifs, as the AHK sequence is known to have an affinity for copper ions, which plays a role in various enzymatic processes within connective tissue. It should be noted that published peer-reviewed research specifically on Pal-AHK as an isolated compound is limited, and much of what is understood about its bioactivity is inferred from related peptide research and cosmetic science literature rather than extensive independent clinical or animal model investigation.
No published research abstracts are currently available for this compound in our database.