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    Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions

    Access Status
    Fulltext not available
    Authors
    Anggayasti, W.
    Mancera, Ricardo
    Bottomley, Steven
    Helmerhorst, Erik
    Date
    2016
    Type
    Journal Article
    
    Metadata
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    Citation
    Anggayasti, W. and Mancera, R. and Bottomley, S. and Helmerhorst, E. 2016. Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions. Analytical Biochemistry. 499: pp. 43-50.
    Source Title
    Analytical Biochemistry
    DOI
    10.1016/j.ab.2015.12.024
    ISSN
    0003-2697
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/42158
    Collection
    • Curtin Research Publications
    Abstract

    © 2016 Elsevier Inc. All rights reserved. Surface plasmon resonance (SPR) is a powerful technique for evaluating protein-protein interactions in real time. However, inappropriately optimized experiments can often lead to problems in the interpretation of data, leading to unreliable kinetic constants and binding models. Optimization of SPR experiments involving "sticky" proteins, or proteins that tend to aggregate, represents a typical scenario where it is important to minimize errors in the data and the kinetic analysis of those data. This is the case of High Mobility Group Box 1 and the receptor of advanced glycation end products. A number of improvements in protein purification, buffer composition, immobilization conditions, and the choice of flow rate are shown to result in substantial improvements in the accurate characterization of the interactions of these proteins and the derivation of the corresponding kinetic constants.

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