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    Design, synthesis, and in vitro inhibitory activity toward human leukocyte elastase, cathepsin G, and proteinase 3 of saccharin-derived sulfones and congeners

    Date
    1996-09-01
    Author
    Groutas, William C.
    Epp, Jeffrey B.
    Venkataraman, Radhika
    Kuang, Rongze
    Truong, Tien M.
    McClenahan, Jerry J.
    Prakash, Om
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    Citation
    Bioorganic & medicinal chemistry. 1996 Sep; 4(9): 1393-400.
    Abstract
    The inhibitory activity toward human leukocyte elastase (HLE), cathepsin G (Cat G), and proteinase 3 (PR 3) of a series of saccharin derivatives having a sulfinate leaving group was investigated. The results of this study revealed that (a) inhibitory activity is dependent on the nature and pKa of the leaving group, and (b) the synthesized saccharin derivatives exhibit selective inhibition toward HLE and PR 3, with low or no activity toward cathepsin G. The results of exploratory biochemical, HPLC and high-field 13C NMR studies are also described.
    Description
    Full text of this article is not available in SOAR.
    URI
    http://hdl.handle.net/10057/4352
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