The coordination of copper(II) to 1-hydroxy-4-(glycyl-histidyl-lysine)-anthraquinone; a synthetic model of anthraquinone anti-cancer drugs.
Pettit. L D LD; Ueda. J J; Morier-Teissier. E E; Helbecque. N N; Bernier. J L JL; Henichart. J P JP; Kozlowski. H H
Key Findings
- Q‑GHK forms a very stable copper complex, mainly using three nitrogen atoms from the peptide (His imidazole and the peptide nitrogens of Gly and His).
- The fourth copper coordination site is likely occupied by the anthraquinone oxygen, adding extra stability.
- At high peptide‑to‑copper ratios, a second Q‑GHK molecule can bind to the copper via its histidine imidazole nitrogen.
Practical Outcomes
- For most biohackers, this research does not provide actionable guidance on using GHK‑Cu or related supplements. It confirms that GHK‑type peptides can strongly chelate copper, but the specific Q‑GHK molecule studied is not used in human health protocols, so no dosage or safety recommendations can be drawn.
Summary
The study shows that a lab‑made version of the GHK peptide attached to an anthraquinone molecule (Q‑GHK) binds copper ions very tightly, forming stable complexes that can generate free radicals and cut DNA. This is mostly a chemistry‑focused investigation and does not test any health‑related effects in people.
Abstract
Results are reported of a pH-metric and spectroscopic (CD and ESR) study of the complexes formed between the pseudo-peptide 1-hydroxy-4-(Gly-His-Lys)-anthraquinone (Q-GHK) since, when complexed to copper ions, Q-GHK has been shown to be very effective in promoting the formation of free radicals and inducing DNA cleavage. Q-GHK forms very stable complexes with copper, the major species being bonded to three nitrogen donors in the coordination plane: an imidazole-N of the His residue and the peptide nitrogens of the Gly and His residues. This species is probably stabilized through bonding of the fourth planar coordination site of Cu(II) to the 9-anthraquinone oxygen. At high Q-GHK:copper ratios a second Q-GHK molecule is coordinated through its imidazole-N donor.
Study Information
pubmed
1992
1992-02-15T00:00:00.000Z
10.1016/0162-0134(92)80045-w