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  • A prodrug approach toward cancer-related carbonic anhydrase inhibition

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    91613_1.pdf (391.4Kb)
    Author(s)
    Carroux, Cindy J
    Rankin, Gregory M
    Moeker, Janina
    Bornaghi, Laurent F
    Katneni, Kasiram
    Morizzi, Julia
    Charman, Susan A
    Vullo, Daniela
    Supuran, Claudiu T
    Poulsen, Sally-Ann
    Griffith University Author(s)
    Poulsen, Sally-Ann
    Year published
    2013
    Metadata
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    Abstract
    The selective inhibition of cancer-associated human carbonic anhydrase (CA) enzymes, specifically CA IX and XII, has been validated as a mechanistically novel approach toward personalized cancer management. Herein we report the design and synthesis of a panel of 24 novel glycoconjugate primary sulfonamides that bind to the extracellular catalytic domain of CA IX and XII. These compounds were synthesized from variably acylated glycopyranosyl azides and either 3- or 4-ethynyl benzene sulfonamide using Cu(I)-catalyzed azide alkyne cycloaddition (CuAAC). The CA enzyme inhibition profile for all compounds was determined, while ...
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    The selective inhibition of cancer-associated human carbonic anhydrase (CA) enzymes, specifically CA IX and XII, has been validated as a mechanistically novel approach toward personalized cancer management. Herein we report the design and synthesis of a panel of 24 novel glycoconjugate primary sulfonamides that bind to the extracellular catalytic domain of CA IX and XII. These compounds were synthesized from variably acylated glycopyranosyl azides and either 3- or 4-ethynyl benzene sulfonamide using Cu(I)-catalyzed azide alkyne cycloaddition (CuAAC). The CA enzyme inhibition profile for all compounds was determined, while in vitro metabolic stability, plasma stability, and plasma protein binding for a representative set of compounds was measured. Our findings demonstrate the influence of the differing acyl groups on these key biopharmaceutical properties, confirming that acyl group protected carbohydrate-based sulfonamides have potential as prodrugs for selectively targeting the extracellular cancer-associated CA enzymes.
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    Journal Title
    Journal of Medicinal Chemistry
    Volume
    56
    Issue
    23
    DOI
    https://doi.org/10.1021/jm401163e
    Copyright Statement
    This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Medicinal Chemistry, copyright 2012 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/jm401163e.
    Subject
    Medicinal and biomolecular chemistry
    Biologically active molecules
    Organic chemistry
    Pharmacology and pharmaceutical sciences
    Publication URI
    http://hdl.handle.net/10072/57021
    Collection
    • Journal articles

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