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  • Plasmodium gametocyte inhibition identified from a natural-product-based fragment library

    Author(s)
    Hoan, Vu
    Roullier, Catherine
    Campitelli, Marc
    Trenholme, Katharine R
    Gardiner, Donald L
    Andrews, Katherine T
    Skinner-Adams, Tina
    Crowther, Gregory J
    Van Voorhis, Wesley C
    Quinn, Ronald J
    Griffith University Author(s)
    Quinn, Ronald J.
    Andrews, Katherine T.
    Skinner-Adams, Tina
    Year published
    2013
    Metadata
    Show full item record
    Abstract
    Fragment-based screening is commonly used to identify compounds with relatively weak but efficient localized binding to protein surfaces. We used mass spectrometry to study fragment-sized three-dimensional natural products. We identified seven securinine-related compounds binding to Plasmodium falciparum 2'-deoxyuridine 5'-triphosphate nucleotidohydrolase (PfdUTPase). Securinine bound allosterically to PfdUTPase, enhancing enzyme activity and inhibiting viability of both P. falciparum gametocyte (sexual) and blood (asexual) stage parasites. Our results provide a new insight into mechanisms that may be applicable to ...
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    Fragment-based screening is commonly used to identify compounds with relatively weak but efficient localized binding to protein surfaces. We used mass spectrometry to study fragment-sized three-dimensional natural products. We identified seven securinine-related compounds binding to Plasmodium falciparum 2'-deoxyuridine 5'-triphosphate nucleotidohydrolase (PfdUTPase). Securinine bound allosterically to PfdUTPase, enhancing enzyme activity and inhibiting viability of both P. falciparum gametocyte (sexual) and blood (asexual) stage parasites. Our results provide a new insight into mechanisms that may be applicable to transmission-blocking agents.
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    Journal Title
    ACS Chemical Biology
    Volume
    8
    Issue
    12
    DOI
    https://doi.org/10.1021/cb400582b
    Copyright Statement
    Self-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the authors for more information.
    Subject
    Chemical sciences
    Biological sciences
    Medical parasitology
    Publication URI
    http://hdl.handle.net/10072/57427
    Collection
    • Journal articles

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