Theoretical study of copper binding to GHK peptide.
Alshammari. Nadiyah N; Platts. James A JA
Key Findings
- Different computational methods (GFN2‑xTB, B3LYP‑D) give consistent low‑energy structures for Cu‑GHK.
- Molecular dynamics shows four equatorial Cu‑N/O bonds stay stable over 100 ps, with the fifth bond to the C‑terminal carboxylate being more fluxional.
- The CREST conformer‑search algorithm can correctly locate the copper binding site starting from separate peptide, copper, and water.
Practical Outcomes
- The work confirms that Cu‑GHK forms a stable complex, supporting its use as a copper‑delivery molecule in supplements or skin products. However, it provides no dosage, safety, or direct usage guidance, so biohackers should treat it as background validation rather than a new protocol.
Summary
Scientists used computer simulations to see how copper ions attach to the GHK peptide. They found that copper binds tightly in four spots around the peptide, while a fifth spot is more flexible, and the modeling tools can reliably predict where copper will sit.
Abstract
We report ligand field molecular mechanics, density functional theory and semi-empirical studies on the binding of Cu(II) to GlyHisLys (GHK) peptide. Following exhaustive conformational searching using molecular mechanics, we show that relative energy and geometry of conformations are in good agreement between GFN2-xTB semi-empirical and B3LYP-D DFT levels. Conventional molecular dynamics simulation of Cu-GHK shows the stability of the copper-peptide binding over 100 ps trajectory. Four equatorial bonds in 3N1O coordination remain stable throughout simulation, while a fifth in apical position from C-terminal carboxylate is more fluxional. We also show that the automated conformer and rotamer search algorithm CREST is able to correctly predict the metal binding position from a starting point consisting of separated peptide, copper and water.
Study Information
pubmed
2020
2020-04-22T00:00:00.000Z
10.1016/j.compbiolchem.2020.107265
5
74