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GHK-Cu Copper Peptide
SKU: GHKCU10M

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Contact Us →GHK-Cu is a synthetic tripeptide-copper complex demonstrating specific molecular interactions in experimental models. The compound consists of glycyl-L-histidyl-L-lysine sequence chelated with copper, showing unique binding properties in laboratory studies. Research indicates selective cellular pathway modulation in controlled experimental conditions.
- High Purity — 99%+ Purity Guaranteed
- Independently Lab Tested
- Research Grade Quality
- For Laboratory Research Use Only
| Chemical Formula | C14H23CuN6O4+ |
|---|---|
| Synonyms | Prezatide copper, Copper peptide, BCP32687, SY253680, GHK copper; CG-copper peptide; [N2-(N-Glycyl-L-histidyl)-L-lysinato(2-)]copper |
| Molar Mass | 402.92 g/mol |
| CAS Number | 89030-95-5 |
| PubChem CID | 78122578 |
| Total Compound Content | 50 mg per vial |
| Shelf Life | 36 months |

What role does the copper(II) ion play in the structure of GHK-Cu?
The copper(II) ion is an essential structural component of GHK-Cu, forming a stable coordination complex through interactions with the Gly-His-Lys tripeptide. This metal-binding arrangement influences the physicochemical properties of the complex and has made GHK-Cu a widely studied model system for investigating copper coordination chemistry, ligand-metal interactions, metallopeptide stability, and copper-dependent signaling mechanisms.
What signaling pathways have been associated with GHK-Cu in experimental investigations?
Research involving GHK-Cu has examined interactions with signaling networks associated with extracellular matrix regulation, structural protein organization, metal-ion transport processes, and peptide-mediated cellular communication. Additional investigations have explored relationships between GHK-Cu and copper-dependent regulatory proteins, redox-associated signaling pathways, and metalloprotein activity, contributing to a broader understanding of metallopeptide signaling systems.
What distinguishes GHK-Cu from other copper-binding peptide complexes?
GHK-Cu combines a well-characterized tripeptide scaffold with high-affinity copper(II) coordination, resulting in a defined metallopeptide structure that has been extensively investigated in coordination chemistry and signaling research. Its established molecular architecture and documented metal-binding properties have made it a valuable reference compound for studies examining ligand-metal interactions, metallopeptide pharmacology, structure-function relationships, and copper-dependent regulatory mechanisms.