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

    Author
    Zhang, F.; Liang, X.; Beaudet, J.M.; Lee, Y.; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    THE EFFECTS OF METAL IONS ON HEPARIN HEPARIN SULFATE-PROTEIN.pdf (1.182Mb)
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    Date Issued
    2014
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    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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    URI
    https://hdl.handle.net/20.500.13015/5321; https://doi.org/10.19104%2Fjbtr.2014.101
    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.;
    Description
    Journal of Biomedical Technology and Research, 1, 1-7; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Publisher
    ELYNS
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;
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    A full text version is available in DSpace@RPI;
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