Carbonless amino acids and a carbonless GHK peptide
Theoretical chemistry paper modeling a boron-nitrogen analogue of GHK and its copper binding; no cell, animal or wound-healing data.
- DFT modeling identified low-energy boron–nitrogen (carbonless) analogues of glycine, histidine and lysine
- The carbonless GHK analogue (cGHK) is predicted to be more conformationally flexible than GHK in water
- cGHK is predicted to bind Cu(II) more strongly than GHK (ΔGexch = -6.24 kcal/mol at 298 K)
Compound: GHK Citation: Skurski P, Anusiewicz I. Phys Chem Chem Phys. 2026;28(14):8675-8691. PubMed
Summary
This is a theoretical, computational chemistry paper. It includes no cell, animal or human experiments, and it does not test hydrogels or wound healing. The authors explore “carbonless” biomolecules: they systematically replace carbon atoms with boron and nitrogen while keeping the same electron count. They apply this to glycine, histidine, lysine and the tripeptide GHK, then use computer models to predict the shapes and copper binding of the resulting analogues.
Key Findings
- DFT calculations (ωB97XD/aug-cc-pVDZ with aqueous solvation), supported by CREST conformer sampling, identified unique low-energy carbonless building blocks: cGly, cHis and cLys
- These were used to build cGHK, a carbonless analogue of GHK
- cGHK is predicted to have a broader range of shapes than GHK under physiological aqueous conditions, meaning it is more conformationally flexible
- Cu(II) binding was modeled with an experimentally supported 3N1O binding motif that includes one water ligand
- The modeling indicates cGHK stabilizes Cu(II) more strongly than GHK (ΔGexch = -6.24 kcal/mol at 298 K)
Relevance to GHK
This paper is only indirectly relevant. It uses GHK’s copper(II) binding as a reference point, which touches the chemistry behind GHK-Cu, but the compound it studies (cGHK) is a computationally designed boron–nitrogen analogue, not GHK. It provides no evidence about GHK’s effects on skin, wounds or healing.
See Also
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