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    Evidence for novel action at the cell-Binding site of human angiogenin revealed by heteronuclear NMR spectroscopy and in silico and in vivo studies.

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    Authors
    Chatzileontiadou, D
    Tsika, A
    Diamantopoulou, Zoi
    Delbé, J
    Badet, J
    Courty, J
    Skamnaki, V
    Parmenopoulou, V
    Komiotis, Dimitri
    Hayes, J
    Spyroulias, G
    Leonidas, D
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    Affiliation
    Department of Biochemistry and Biotechnology, University of Thessaly, Biopolis, 41500, Larissa, Greece
    Issue Date
    2018-01-04
    
    Metadata
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    Abstract
    A member of the ribonuclease A superfamily, human angiogenin (hAng) is a potent angiogenic factor. Heteronuclear NMR spectroscopy combined with induced-fit docking revealed a dual binding mode for the most antiangiogenic compound of a series of ribofuranosyl pyrimidine nucleosides that strongly inhibit hAng's angiogenic activity in vivo. While modeling suggests the potential for simultaneous binding of the inhibitors at the active and cell-binding sites, NMR studies indicate greater affinity for the cell-binding site than for the active site. Additionally, molecular dynamics simulations at 100 ns confirmed the stability of binding at the cell-binding site with the predicted protein-ligand interactions, in excellent agreement with the NMR data. This is the first time that a nucleoside inhibitor is reported to completely inhibit the angiogenic activity of hAng in vivo by exerting dual inhibitory activity on hAng, blocking both the entrance of hAng into the cell and its ribonucleolytic activity.
    Citation
    Evidence for novel action at the cell-Binding site of human angiogenin revealed by heteronuclear NMR spectroscopy and in silico and in vivo studies. 2018 ChemMedChem
    Journal
    ChemMedChem
    URI
    http://hdl.handle.net/10541/620811
    DOI
    10.1002/cmdc.201700688
    PubMed ID
    29314771
    Type
    Article
    Language
    en
    ISSN
    1860-7187
    ae974a485f413a2113503eed53cd6c53
    10.1002/cmdc.201700688
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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