AHK (Tripeptide-3) 200mg (Topical)

AHK (Tripeptide-3) is a short synthetic peptide consisting of three amino acids: alanine, histidine, and lysine. Due to the presence of histidine, the peptide may form complexes with copper ions in certain experimental contexts, resulting in AHK-Cu. In laboratory research, AHK is evaluated for its influence on cellular signaling pathways associated with extracellular matrix regulation, angiogenic signaling, and tissue remodeling processes.

Most published work utilizes in vitro cell culture systems and animal models to examine how AHK modulates fibroblast behavior, endothelial cell activity, and growth factor expression. Investigations frequently focus on transcriptional and protein-level changes linked to collagen production, vascular-associated markers, and regulatory cytokines. Within experimental frameworks, AHK functions as a research tool for studying peptide-driven signaling mechanisms involved in connective tissue and vascular biology.

Sequence (Three-Letter Code): Ala-His-Lys
Molecular formula: C15H26N6O4
Molecular weight: 354.41 g/mol

The histidine residue within the AHK sequence provides a metal-coordination site, which enables reversible complexation with copper ions in experimental settings. This property has made AHK a frequent subject of structure–function studies examining how short peptides interact with metal cofactors and influence downstream biochemical behavior.

Research applications for AHK are primarily conducted in vitro using cultured dermal fibroblasts, endothelial cells, and hair follicle–associated cell systems, as well as in animal models designed to evaluate tissue remodeling. Experimental designs typically compare peptide-treated samples to untreated or vehicle-treated controls to quantify changes in gene expression, protein synthesis, and cellular proliferation markers.

Commonly measured endpoints include collagen type I and extracellular matrix protein expression, growth factor–related markers such as vascular endothelial growth factor (VEGF), transforming growth factor beta-1 (TGF-β1), and indicators of endothelial cell migration or proliferation. In hair follicle–focused models, investigators may evaluate dermal papilla cell activity, follicular elongation parameters, and vascular density markers relative to controls.

Across all study systems, reported findings are interpreted as mechanistic observations within laboratory settings. Results are limited to in vitro and animal research contexts and do not imply cosmetic, clinical, or human use.

Fibroblasts are central regulators of connective tissue architecture through their production of ECM proteins, including collagen and elastin. These cells also secrete signaling molecules that influence endothelial behavior and vascular development. Endothelial cells, in turn, participate in angiogenic and maintenance programs governed by growth factor signaling networks.

Mechanistic studies have examined AHK-mediated modulation of VEGF-linked signaling cascades and TGF-β1–associated transcriptional programs. These pathways are commonly studied in preclinical systems to understand how short peptides influence fibroblast–endothelial cross-talk and ECM remodeling under controlled laboratory conditions.

In vitro and animal-model studies have evaluated AHK as a regulator of fibroblast-associated ECM synthesis. In cultured dermal fibroblasts, exposure to AHK has been associated with increased collagen type I expression under specific experimental conditions, supporting its use as a mechanistic probe in collagen-related research [1].

Additional preclinical investigations have explored AHK-driven modulation of angiogenesis-related signaling, including effects on endothelial growth factor expression and vascular-associated cellular responses in experimental hair follicle models [2,3]. These studies are frequently cited to contextualize AHK within broader connective tissue and vascular biology research frameworks.

AHK (Tripeptide-3) is supplied as a purified research reagent intended for laboratory experimentation. Product identity and purity are typically confirmed using analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry (MS). Standard peptide handling and storage practices should be followed in research environments.

1. neova-dna-nourishing-study.pdf. Available at: http://www.dermacaredirect.co.uk/skin/frontend/default/dermacare/pdf/neova-dna-nourishing-study.pdf. (Accessed: 25th July 2016)
2. Pyo, H. K. et al. The effect of tripeptide-copper complex on human hair growth in vitro. Arch. Pharm. Res. 30, 834–839 (2007).
3. Pollard, J. D., Quan, S., Kang, T. & Koch, R. J. Effects of copper tripeptide on the growth and expression of growth factors by normal and irradiated fibroblasts. Arch. Facial Plast. Surg. 7, 27–31 (2005).

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The products offered on this website are furnished for in-vitro studies only. In-vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law.

For Laboratory Research Only. Not for human use, medical use, diagnostic use, or veterinary use.