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    Differential Effects of Methoxy Group on the Interaction of Curcuminoids with Two Major Ligand Binding Sites of Human Serum Albumin

    245558_195108.pdf (4.987Mb)
    Access Status
    Open access
    Authors
    Sato, H.
    Chuang, Victor
    Yamasaki, K.
    Yamaotsu, N.
    Watanabe, H.
    Nagumo, K.
    Anraku, M.
    Kadowaki, D.
    Ishima, Y.
    Hirono, S.
    Otagiri, M.
    Maruyama, T.
    Date
    2014
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Sato, H. and Chuang, V. and Yamasaki, K. and Yamaotsu, N. and Watanabe, H. and Nagumo, K. and Anraku, M. et al. 2014. Differential Effects of Methoxy Group on the Interaction of Curcuminoids with Two Major Ligand Binding Sites of Human Serum Albumin. PLoS ONE. 9 (2).
    Source Title
    PLoS ONE
    DOI
    10.1371/journal.pone.0087919
    ISSN
    1932-6203
    School
    School of Pharmacy
    Remarks

    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/4.0/. Please refer to the licence to obtain terms for any further reuse or distribution of this work.

    URI
    http://hdl.handle.net/20.500.11937/17812
    Collection
    • Curtin Research Publications
    Abstract

    Curcuminoids are a group of compounds with a similar chemical backbone structure but containing different numbers of methoxy groups that have therapeutic potential due to their anti-inflammatory and anti-oxidant properties. They mainly bind to albumin in plasma. These findings influence their body disposition and biological activities. Spectroscopic analysis using site specific probes on human serum albumin (HSA) clearly indicated that curcumin (Cur), demethylcurcumin (Dmc) and bisdemethoxycurcumin (Bdmc) bind to both Site I (sub-site Ia and Ib) and Site II on HSA. At pH 7.4, the binding constants for Site I were relatively comparable between curcuminoids, while the binding constants for Site II at pH 7.4 were increased in order Cur , Dmc , Bdmc. Binding experiments using HSA mutants showed that Trp214 and Arg218 at Site I, and Tyr411 and Arg410 at Site II are involved in the binding of curcuminoids. The molecular docking of all curcuminoids to the Site I pocket showed that curcuminoids stacked with Phe211 and Trp214, and interacted with hydrophobic and aromatic amino acid residues. In contrast, each curcuminoid interacted with Site II in a different manner depending whether a methoxy group was present or absent. A detailed analysis of curcuminoids-albumin interactions would provide valuable information in terms of understanding the pharmacokinetics and the biological activities of this class of compounds.

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