AHK-Cu
/ Copper-binding tripeptide; alanyl-histidyl-lysine copper complex (analog of GHK-Cu)ALIAS · AHK-Cu · Alanyl-Histidyl-Lysine Copper · AHK copper tripeptide
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Tier 3. AHK-Cu is the alanyl-histidyl-lysine copper(II) tripeptide complex, a structural analog of the better-studied GHK-Cu (glycyl-histidyl-lysine copper). Established research peptide in the Pickart group's wider copper-tripeptide programme, with specific interest in hair-follicle biology — proliferation of dermal papilla cells and follicle protein expression in vitro. Less-studied than GHK-Cu and with a smaller indexed-literature footprint.
AHK-Cu is a copper(II) chelate of the synthetic tripeptide alanyl-histidyl-lysine. As with the related GHK-Cu, the histidine and amide nitrogens coordinate the copper centre, producing a soluble peptide-copper complex with redox and signalling activities distinct from either the free peptide or free copper alone. The principal published activity in the cosmetic and dermatological literature concerns dermal papilla cell proliferation and modulation of hair-follicle-associated gene expression in vitro, with proposed application to hair-loss endpoints.
Tier 3 (animal / in vitro). The published characterisation is principally in-vitro cell-culture work on dermal papilla cells and rodent follicle preparations, in continuity with the Pickart group's broader copper-tripeptide programme. Human-trial data specific to AHK-Cu are limited.
No formal independent human safety database for AHK-Cu specifically. Class-level safety inference from GHK-Cu (which has more substantial cosmetic-use exposure) is the closest available proxy and is not a substitute for direct AHK-Cu data.
Regulatory status
- FDA status:
- Not FDA-approved
The specific evidence base for AHK-Cu is much thinner than that for the parent GHK-Cu, although vendor and review literature commonly conflates the two. Independent replication outside the originating research lineage is limited. Topical formulation, copper-loading, and stability of vendor product are not tightly constrained by any external standard.