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  • D-tyrosine as a chiral precusor to potent inhibitors of human nonpancreatic secretory phospholipase A2 (IIa) with antiinflammatory activity

    Author(s)
    Hansford, KA
    Reid, RC
    Clark, CI
    Tyndall, JDA
    Whitehouse, MW
    Guthrie, T
    McGeary, RP
    Schafer, K
    Martin, JL
    Fairlie, DP
    Griffith University Author(s)
    Martin, Jennifer
    Year published
    2003
    Metadata
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    Abstract
    Few reported inhibitors of secretory phospholipase A2enzymes truly inhibit the IIa human isoform (hnpsPLA2-IIa) noncovalently at submicromolar concentrations. Herein, the simple chiral precursor D-tyrosine was derivatised to give a series of potent new inhibitors of hnpsPLA2-IIa. A 2.2-Å crystal structure shows an inhibitor bound in the active site of the enzyme, chelated to a Ca2+ion through carboxylate and amide oxygen atoms, H-bonded through an amide NH group to His48, with multiple hydrophobic contacts and a T-shaped aromatic-group–His6 interaction. Antiinflammatory activity is also demonstrated for two compounds ...
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    Few reported inhibitors of secretory phospholipase A2enzymes truly inhibit the IIa human isoform (hnpsPLA2-IIa) noncovalently at submicromolar concentrations. Herein, the simple chiral precursor D-tyrosine was derivatised to give a series of potent new inhibitors of hnpsPLA2-IIa. A 2.2-Å crystal structure shows an inhibitor bound in the active site of the enzyme, chelated to a Ca2+ion through carboxylate and amide oxygen atoms, H-bonded through an amide NH group to His48, with multiple hydrophobic contacts and a T-shaped aromatic-group–His6 interaction. Antiinflammatory activity is also demonstrated for two compounds administered orally to rats.
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    Journal Title
    ChemBioChem
    Volume
    4
    Issue
    2-3
    DOI
    https://doi.org/10.1002/cbic.200390029
    Subject
    Medicinal and biomolecular chemistry
    Medicinal and biomolecular chemistry not elsewhere classified
    Biochemistry and cell biology
    Publication URI
    http://hdl.handle.net/10072/347898
    Collection
    • Journal articles

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