The effects of metal ions on heparin/heparin sulfate-protein interactions

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Authors
Zhang, F.
Liang, X.
Beaudet, J.M.
Lee, Y.
Linhardt, Robert J.
Issue Date
2014
Type
Article
Language
ENG
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Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Abstract
Heparin/heparin sulfate (HS) interacts with a number of proteins thereby playing an essential role in the regulation of many physiological processes. The understanding of heparin/HS-protein interactions at the molecular level is of fundamental importance to biology and will aid in the development of highly specific glycan-based therapeutic agents. The heparin-binding proteins (HBPs) interact with sulfated domains of heparin/HS chains primarily through ionic attraction between negatively charged groups in HS/heparin chains and basic amino acid residues within the protein. Reports in literature have been shown that heparin molecules have a high affinity for a wide range of metal ions. In the present study, we used surface plasmon resonance (SPR) to study the effects of metal ions (under physiological and non-physiological concentrations) on heparin/HS-protein interactions. The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7). While the effects of individual metal ion at physiological concentrations had little impact on protein binding, the mixed metal ions reduced the FGF1/heparin or IL7/heparin binding affinity, changing its binding profile.
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Journal of Biomedical Technology and Research, 1, 1-7
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Full Citation
The effects of metal ions on heparin/heparin sulfate-protein interactions, F. Zhang, X. Liang, J. M. Beaudet, Y. Lee, R. J. Linhardt, Journal of Biomedical Technology and Research, 1, 1-7, 2014
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ELYNS
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