AHK-Cu

AHK-Cu is a synthetic copper-binding tripeptide composed of alanine, histidine, and lysine. It is classified as a tripeptide-copper complex structurally related to GHK-Cu, differing in the substitution of alanine for glycine at the N-terminus. AHK-Cu is investigated in cosmetic peptide research and hair follicle research models.

In biological systems, AHK binds copper ions to form the bioactive AHK-Cu complex, which functions as a signaling molecule in cellular research models. The peptide engages copper-dependent enzymatic processes, supports endothelial-related cellular responses, and has been studied for its influence on dermal papilla cell signaling pathways. The compact tripeptide-copper structure positions AHK-Cu as a useful comparative research compound alongside other copper-binding peptides.

Research interest in AHK-Cu focuses on hair follicle research, dermal papilla cell models, VEGF and angiogenic-pathway signaling research, and copper-dependent cellular signaling. Comparative research with GHK-Cu explores how the N-terminal residue substitution influences copper-peptide signaling profiles in cellular-pathway research and cosmetic peptide research contexts.

The peptide is supplied as a lyophilized powder to ensure optimal stability during storage and handling.

AHK is a tripeptide composed of alanine, histidine, and lysine. The AHK-Cu complex forms when AHK binds a copper ion, creating a bioactive copper-peptide signaling molecule that has been studied alongside the more extensively characterized GHK-Cu tripeptide. The two compounds share the histidine-lysine C-terminal motif required for copper coordination, but differ at the N-terminus, where AHK substitutes alanine for the glycine residue found in GHK.

Experimental studies have investigated AHK-Cu in dermal papilla cell research models, where it has been examined for its influence on growth-related signaling and VEGF-pathway expression. AHK-Cu is also investigated for copper transport, antioxidant defense pathway research, and cellular-pathway signaling within cosmetic and dermatological research contexts.

The structural similarity to GHK-Cu and the substitution of alanine for glycine at the N-terminus has positioned AHK-Cu as a useful comparative research compound for laboratory studies of copper-peptide pharmacology, hair follicle research, and follicle-pathway research.

1. Copper Transport and Delivery

AHK binds copper ions and facilitates their safe transport and delivery to cellular research models, supporting copper-dependent enzymatic processes essential for cellular-process research and antioxidant defense research.

2. Dermal Papilla Cell Signaling Research

AHK-Cu has been investigated in hair follicle research models, particularly dermal papilla cell cultures, where it is studied for its role in growth-related signaling and cellular activity in follicle-pathway research.

3. VEGF and Vascular Pathway Research

Research has examined AHK-Cu for its association with VEGF (vascular endothelial growth factor) expression and angiogenic-pathway signaling in cellular models, which is relevant to follicle research and dermal cellular-pathway research contexts.

4. Comparative Copper-Peptide Research

AHK-Cu is frequently studied alongside GHK-Cu as a comparative copper-peptide research compound, allowing investigation of how N-terminal residue substitution (alanine versus glycine) influences copper-peptide signaling profiles in cellular research models.

Research Applications

Conclusion

AHK-Cu is a copper-binding tripeptide investigated for its role in hair follicle research, copper transport, and comparative copper-peptide pharmacology research. Its structural similarity to GHK-Cu and substitution of alanine for glycine at the N-terminus makes AHK-Cu a useful research compound for laboratory studies of copper-peptide signaling and follicle-related research models.

Research Use Disclaimer

This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.