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Cited by 80Protein Interaction Studies and Fluorescence AnalysisMetal complexes synthesis and propertiesTrace Elements in Health

The interaction of copper(II) and glycyl-l-histidyl-l-lysine, a growth-modulating tripeptide from plasma

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Lau, S J, Sarkar, B·1981·Biochemical Journal
DOI 10.1042/bj1990649PMC PMC1163421
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Abstract

The interaction between Cu(II) and the growth-modulating tripeptide glycyl-L-histidyl-L-lysine in the presence and absence of L-histidine was investigated by potentiometric titration and visible-absorption spectrophotometry at 25 degrees C in 0.15 M-NaCl. Analyses of the results in the pH range 3.5--10.6 indicated the presence of multiple species in solution in the binary system and extensive amounts of the ternary complexes in the ternary system. The species distribution and the stability constants, as well as the visible-absorption spectra of the species, were evaluated. The combined results were used to propose the structure of some of the complexes. The influence of the epsilon-amino group of the peptide in the enhancement of the stability constants was reflected prominently when compared with those complexes formed by either glycyl-L-histidine or glycyl-L-histidylglycine. The results obtained from the equilibrium-dialysis experiments showed that this tripeptide was able to compete with albumin for Cu(II) at pH 7.5 and 6 degrees C. At equimolar concentrations of albumin and the peptide, about 42% of the Cu(II) was bound to the peptide. At the physiologically relevant concentrations of Cu(II), albumin, L-histidine and this peptide, about 6% of the Cu(II) was associated with the low-molecular-weight components. This distribution could be due to the binary as well as the ternary complexes. The possible physiological role of these complexes in the transportation of Cu(II) from blood to tissues is discussed.

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  • GHK can obtain copper ions bound to other molecules such as albumin and serve as a delivery vehicle for copper ions locally, for example, at a site of injury.

    “Since albumin is the main copper-transporting molecule in human plasma, GHK's ability to obtain copper ions from albumin enables it to serve as a delivery vehicle for copper ions locally, for example, in a site of an injury [11].”

    From GHK-Cu may Prevent Oxidative Stress in Skin by Regulating Copper and Modifying Expression of Numerous Antioxidant Genes (2015) · cites this paper as [11]

    The Discussion reports that GHK removes Cu(II) from a copper–albumin complex and suggests that GHK may help deliver copper from blood to tissues. It does not establish delivery specifically at an injury site. The Abstract also says that 90–95% of plasma copper is bound to caeruloplasmin, so it does not support an unqualified description of albumin as the main copper-binding molecule in plasma. Page numbers were not supplied for these passages. (LLM, conf=0.87)

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  • The paper's calculated protonation and formation constants are closest to those obtained by Lau et al. and Conato et al., two groups that also utilised potentiometry.

    “Our calculated protonation and formation constants values are closest to those obtained by Lau et al. [28] and Conato et al. [18], two groups that also utilised potentiometry to calculate the binding constants.”

    From Ternary Cu(II) Complex with GHK Peptide and Cis-Urocanic Acid as a Potential Physiologically Functional Copper Chelate (2020) · cites this paper as [28]

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Cites

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Research works printed but not linked: 4

  1. [1]1. Agarwal, R. P. & Perrin, D. D. (1975) J. Chem. Soc. Dalton Trans. 268-272
  2. [2]2. Bearn, A. G. & Kunkel, H. G. (1954) Proc. Soc. Exp. Biol. Med. 88,44-48
  3. [11]11. Lau, S. & Sarkar, B. (1981) J. Chem. Soc. Dalton Trans. 491-494
  4. [21]21. Sarkar, B. & Kruck, T. P. A. (1966) in Biochemistry of Copper (Peisach, J., Aisen, P. & Blumberg, W. E., eds.), pp. 183-196, Academic Press, New York

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Authors
Lau, S. J., & Sarkar, B.
Affiliations
University of Toronto (CA)
ORCID
Sarkar, B
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
1981-12-01
Volume
199
Issue
3
Pages
649-656
ISSN
0264-6021 (ISSN-L)
DOI
10.1042/bj1990649
PMC
PMC1163421
OpenAlex
W2109330288
Cited by
79
References
15
Citations by year
2026: 2 · 2025: 2 · 2023: 3 · 2022: 1 · 2021: 4 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 1 · 2016: 4 · 2015: 2 · 2012: 1
FWCI
1.24
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
  • Health Sciences › Medicine › Oncology › Metal complexes synthesis and properties
  • Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords
copper(II) complexes, tripeptides, histidine, stability constants, species distribution, epsilon-amino groups, albumin, copper transport, plasma peptides
MeSH terms
Copper, Dialysis, Growth Substances, Histidine, Humans, Oligopeptides, Potentiometry, Serum Albumin, Spectrophotometry, Macromolecular Substances

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