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GHK-Cu

Copper Tripeptide-1, Glycyl-L-Histidyl-L-Lysine Copper, Prezatide Copper

Quick Stats
Studies 149
Trials 1
Score 3
1980 pubmed

Growth-modulating plasma tripeptide may function by facilitating copper uptake into cells.

Pickart. L L; Freedman. J H JH; Loker. W J WJ; Peisach. J J; Perkins. C M CM; Stenkamp. R E RE; Weinstein. B B

Key Findings

  • GHK/GHL readily forms complexes with copper (and some iron) at nanomolar concentrations.
  • When added to cultured hepatoma (liver) cells, the peptide significantly increases copper uptake into the cells.
  • Tripeptides with a histidine‑lysine linkage show similar activity, indicating the histidine next to a basic residue is crucial for copper transport.

Practical Outcomes

  • For biohackers, the data supports the idea that GHK‑Cu can act as a copper‑delivery agent, potentially enhancing copper‑dependent processes like antioxidant enzyme function. However, because the work is limited to cell cultures, there are no proven human dosing guidelines yet. If experimenting, start with very low (nanomolar‑equivalent) doses used in research and monitor copper status to avoid excess.

Summary

The study shows that a tiny tripeptide (called GHK or GHL) can grab copper ions and help cells pull the metal inside. In lab-grown liver cells, adding the peptide with copper made the cells take up more copper, suggesting the peptide works like a natural copper‑carrier. This explains why GHK‑Cu supplements might boost copper delivery in the body, but the research is still at the cell‑culture stage.

Abstract

The plasma tripeptide glycyl-L-lysine (GHL), when added at nanomolar concentrations to a wide group of cultured systems, produces a disparate set of responses ranging from the stimulation of growth and differentiation to outright toxicity. Such diverse actions imply that this tripeptide mediates some basic biochemical function common to many types of cells and organisms. During the isolation of GHL we found the compound to co-isolate through a number of steps with approximately equimolar copper and about 1/5 molar iron. Maximal effects on hepatoma cells (HTC4) were seen when the peptide was added with copper and iron to the growth medium. Structure-function studies revealed that several tripeptides with a histidyl-lysyl linkage were nearly as active as GHL. The association of GHL with copper and a homology similarity between the tripeptide and the copper transport sites on albumin and alpha-fetoprotein, where the cupric atom is bound to a histidyl residue adjacent to a basic residue, suggested that GHL may act as a copper transport factor. We report here that the tripeptide readily forms complexes with copper(II) and enhances the uptake of the metal into cultured hepatoma cells.

Study Information

Provider

pubmed

Year

1980

Date

1980-12-25T00:00:00.000Z

DOI

10.1038/288715a0