Research Overview
Two tripeptides, one coordination motif
GHK and AHK differ only at the first residue — glycine versus alanine — and both rely on the His-Lys pair for copper binding. The imidazole nitrogen of histidine, the terminal amine and backbone nitrogens together form the square-planar Cu(II) site, and the resulting complex has an affinity comparable to that of serum albumin's copper-transport site. That similarity is why GHK-Cu is often discussed as a physiological copper carrier rather than simply a copper salt in peptide clothing.
Follicle research
Why formulation matters here
- Copper coordination is pH sensitive; strongly acidic conditions dissociate the complex
- Reducing agents such as ascorbic acid and thiol compounds can reduce Cu(II) and disrupt the peptide complex
- Chelators including EDTA compete for copper and strip it from the tripeptide
- Free copper ions behave very differently from the coordinated complex in cell assays
- Colour loss is a practical, if rough, in-bottle indicator that the active has changed