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    Photoaffinity labeling of plasma proteins

    193348_97701_Chuang_Mol_2013.pdf (1.917Mb)
    Access Status
    Open access
    Authors
    Chuang, Victor
    Otagiri, M.
    Date
    2013
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Chuang, Victor Tuan Giam and Otagiri, Masaki. 2013. Photoaffinity labeling of plasma proteins. Molecules. 18 (11): pp. 13831-13859.
    Source Title
    Molecules
    DOI
    10.3390/molecules181113831
    ISSN
    1420-3049
    Remarks

    Published by MDPI Publishing

    This article is published under the Open Access publishing model and distributed under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/. Please refer to the licence to obtain terms for any further reuse or distribution of this work.

    URI
    http://hdl.handle.net/20.500.11937/33694
    Collection
    • Curtin Research Publications
    Abstract

    Photoaffinity labeling is a powerful technique for identifying a target protein. A high degree of labeling specificity can be achieved with this method in comparison to chemical labeling. Human serum albumin (HSA) and α1-acid glycoprotein (AGP) are two plasma proteins that bind a variety of endogenous and exogenous substances. The ligand binding mechanism of these two proteins is complex. Fatty acids, which are known to be transported in plasma by HSA, cause conformational changes and participate in allosteric ligand binding to HSA. HSA undergoes an N-B transition, a conformational change at alkaline pH, that has been reported to result in increased ligand binding. Attempts have been made to investigate the impact of fatty acids and the N-B transition on ligand binding in HSA using ketoprofen and flunitrazepam as photolabeling agents. Meanwhile, plasma AGP is a mixture of genetic variants of the protein. The photolabeling of AGP with flunitrazepam has been utilized to shed light on the topology of the protein ligand binding site. Furthermore, a review of photoaffinity labeling performed on other major plasma proteins will also be discussed. Using a photoreactive natural ligand as a photolabeling agent to identify target protein in the plasma would reduce non-specific labeling.

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