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GHK-Cu: Research Overview

PūrTONIX Analytical Team3 min read
02

Compound Overview

Full name
Glycyl-L-histidyl-L-lysine copper(II) complex
Molecular formula
C14H24CuN6O4
Molecular weight
403.92 g/mol
Sequence / class
Tripeptide-copper(II) complex; glycine-histidine-lysine sequence coordinated to a single Cu(II) center
Receptor targets
Direct copper-ion delivery to cellular copper-binding proteins and metalloenzymes; published in vitro literature also describes downstream effects on extracellular matrix gene expression in cellular models
Research classification
Copper-binding tripeptide research reagent for in vitro studies of copper biochemistry and matrix-protein signaling
PubChem CID
133472

GHK-Cu is a copper-binding tripeptide complex consisting of the glycine-histidine-lysine peptide sequence coordinated to a divalent copper(II) ion. The molecular formula is C14H24CuN6O4 with a molecular weight near 404 daltons. The peptide binds copper through the imidazole nitrogen of histidine, the alpha-amino group of glycine, and the deprotonated amide nitrogen between glycine and histidine, forming a square-planar coordination geometry that has been characterized in publicly available crystallographic and spectroscopic databases.

Published literature classifies GHK-Cu as a copper-delivery tripeptide research reagent. The complex serves as an analytical probe for studying copper-ion biochemistry in cellular models, with published in vitro research describing effects on extracellular matrix gene expression, fibroblast-line behavior, and copper-dependent enzyme activity under controlled buffer conditions.

Research published in the peer-reviewed literature has used GHK-Cu in cellular research contexts where controlled copper delivery is required. The peptide-coordinated form is reported to deliver copper to cellular systems with kinetics that differ from those of inorganic copper salts, providing investigators with an analytical tool for studying how the form of copper presentation influences downstream cellular biochemistry.

Published research suggests that GHK-Cu engages multiple pathway-level effects in cellular models rather than acting through a single receptor target. This breadth of in vitro effects reflects the central role of copper biochemistry in cellular metalloenzyme function and in the regulation of several matrix-protein gene expression programs documented in publicly available literature.

03

Molecular Structure

GlyHisLysCu²⁺Square-planar Cu(II) coordination
GHK-Cu
C14H24CuN6O4
Molecular weight 403.92 g/mol

Structure reference: Public domain chemical databases (PubChem CID 133472).

04

In Vitro Research Applications

The following applications reflect published in vitro and preclinical research only. None of these applications constitute approved medical use.

Published in vitro applications of GHK-Cu include its use in fibroblast-line gene-expression studies, in vitro extracellular-matrix protein synthesis assays, and copper-loading studies of cellular metalloenzymes. Investigators have used the complex as a controlled copper-delivery reagent when comparing the behavior of peptide-bound copper against inorganic copper salt presentations in matched cellular models.

Research published in cellular biology journals has examined the kinetics of copper transfer from the GHK-Cu complex to cellular copper-binding proteins, including ceruloplasmin and superoxide dismutase under defined buffer conditions. These studies frame the tripeptide as an analytical probe for copper biochemistry rather than as a ligand for a classical signaling receptor.

Additional published in vitro literature describes the use of GHK-Cu in cellular signaling research on extracellular matrix biochemistry, with collagen, decorin, and elastin gene-expression readouts used as standard analytical endpoints in cultured fibroblast model systems.

05

Published Research Highlights

  • [1]A study published in Biochemical Journal (1988) examined the copper-coordination biochemistry of the glycine-histidine-lysine tripeptide using publicly available analytical methods.
  • [2]A study published in FEBS Letters (1990) investigated GHK-Cu effects on extracellular matrix gene expression in cellular fibroblast model systems.
  • [3]A study published in BioMed Research International (2014) reviewed publicly available in vitro literature on GHK-Cu and copper-tripeptide complex biochemistry.

The above represents a non-exhaustive summary of publicly available research. PūrTONIX does not endorse, validate, or make claims based on any referenced study.

06

Analytical Considerations for Laboratory Use

Published chemical property data indicate that GHK-Cu is soluble in water and in mildly buffered aqueous solutions at neutral to slightly alkaline pH, conditions that preserve the copper-coordination geometry. The lyophilized complex is stored at -20°C under inert atmosphere, with reconstituted stocks held in single-use aliquots to minimize oxidative copper-state changes during repeated freeze-thaw cycles.

Reconstitution for in vitro use is standard in aqueous buffer matched to the intended cellular assay. Analytical characterization of research-grade material commonly includes reverse-phase HPLC purity analysis, UV-Vis spectroscopy confirming the characteristic copper-complex absorption near 550 nm, and quantitative copper content measurement by atomic absorption or ICP-MS.

Handling recommendations are based on published chemical property data and are intended for qualified laboratory personnel only.

07

Research-Grade Sourcing Standards

Copper-coordination chemistry is sensitive to lot-level peptide purity and to the precise copper-to-peptide stoichiometry. Well-characterized material is typically documented for chromatographic purity and quantitative copper content.

Laboratory Research Reagents · Not for Human or Veterinary Use