Extracellular Matrix Models
Copper peptide complexes have been studied for effects on collagen, elastin, and glycosaminoglycan signaling in dermal fibroblast and tissue culture models.
Overview
What is AHK-CU?
AHK-CU is a copper-binding tripeptide related to the broader family of copper peptide complexes studied in extracellular matrix biology, dermal fibroblast signaling, and tissue remodeling models. Research has examined copper peptide complexes for their interactions with collagen synthesis pathways, angiogenic signaling, and cellular repair responses in controlled laboratory systems.
AHK-CU (L-Alanyl-L-Histidyl-L-Lysine Copper) is supplied strictly as a reference material for in vitro and preclinical investigation. All characterization data described here is drawn from peer-reviewed literature and laboratory analysis; nothing herein constitutes a claim of clinical effect in humans.
Investigational Scope
Documented Research Areas
The following domains summarize directions explored across published studies and laboratory models. Each reflects observations reported in rodent models, in vitro systems, or the peer-reviewed record.
Trace Metal Complex Research
AHK-CU provides a defined peptide-copper complex for investigations into copper delivery, peptide coordination chemistry, and downstream cellular responses.
Fibroblast Signaling
Laboratory studies of related copper peptides have examined fibroblast activity, matrix turnover markers, and tissue remodeling pathways.
Vascular Signaling Models
Copper-dependent pathways are frequently examined in angiogenesis and wound biology models where matrix remodeling and vascular signaling overlap.
Proposed Mechanism
Mechanistic Pathway
Mechanistic steps below are hypothesized from in vitro assays and animal-model data reported in the literature. They describe biochemical interactions observed under controlled experimental conditions.
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1
Copper Coordination
The AHK sequence coordinates copper ions through histidine and terminal amine groups, creating a stable complex for controlled peptide-metal research.
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2
Matrix Gene Signaling
Copper peptide complexes are studied for modulation of genes associated with collagen synthesis, extracellular matrix turnover, and fibroblast activity.
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3
Metalloprotein Interaction
Copper availability can influence metalloprotein function and oxidative enzyme systems that participate in tissue remodeling models.
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4
Cellular Repair Pathways
Researchers use copper peptide complexes to examine signaling networks associated with repair, migration, and matrix deposition under laboratory conditions.
Technical Data
Molecular Specifications
| Amino Acid Sequence | Ala-His-Lys complexed with copper |
|---|---|
| Molecular Weight | 403.9 g/mol |
| Molecular Formula | C12H22CuN6O4 |
| CAS Number | 49557-75-7 |
| Storage | -20°C long-term, 4°C short-term up to 4 weeks |
References
Selected Literature
The following peer-reviewed references informed the research summaries on this page. Citations are provided for scientific context only.
- Pickart L & Margolina A. (2018). Regenerative and protective actions of the GHK-Cu peptide. International Journal of Molecular Sciences, 19(7), 1987.
- Pickart L. (2008). The human tri-peptide GHK and tissue remodeling. Journal of Biomaterials Science, Polymer Edition, 19(8), 969-988.
- Gruchlik A, et al. (2014). The effect of copper complexes on collagen biosynthesis in skin fibroblasts. Pharmacological Reports, 66(6), 1047-1052.
- Borkow G. (2014). Using copper to improve the well-being of the skin. Current Chemical Biology, 8(2), 89-102.
- Linder MC. (2016). Ceruloplasmin and other copper binding components of blood plasma and their functions. Metallomics, 8(9), 887-905.
Research Disclaimer
This product is intended strictly for laboratory research purposes only. It is not a drug, food, cosmetic, or dietary supplement and is not intended to diagnose, treat, cure, or prevent any disease. It is not for human or animal consumption. All information presented is derived from published scientific literature and is provided for educational reference only. By purchasing, the buyer affirms they are a qualified researcher or institution and assume full responsibility for the safe and lawful handling of this material.