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Issue 18, 2010
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Design and synthesis of nonpeptidic, small molecule inhibitors for the Mycobacterium tuberculosis protein tyrosine phosphatase PtpB

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Abstract

The design and synthesis of new inhibitor analogues for the Mycobacterium tuberculosis (Mtb) phosphatase PtpB is described. Analogues were synthesized by incorporation of two common and effective phosphate mimetics, the isothiazolidinone (IZD) and the difluoromethylphosphonic acid (DFMP). The basic scaffold of the inhibitor was identified from structure–activity relationships established for a previously published isoxazole inhibitor, while the phosphate mimetics were chosen based on their proven cell permeability and activity when incorporated into previously reported inhibitors for the phosphatase PTP1B. The inhibitory activity of each compound was evaluated, and each was found to have low or submicromolar affinity for PtpB.

Graphical abstract: Design and synthesis of nonpeptidic, small molecule inhibitors for the Mycobacterium tuberculosis protein tyrosine phosphatase PtpB

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Publication details

The article was received on 28 May 2010, accepted on 01 Jul 2010 and first published on 19 Jul 2010


Article type: Communication
DOI: 10.1039/C0OB00182A
Citation: Org. Biomol. Chem., 2010,8, 4066-4070
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    Design and synthesis of nonpeptidic, small molecule inhibitors for the Mycobacterium tuberculosis protein tyrosine phosphatase PtpB

    K. A. Rawls, C. Grundner and J. A. Ellman, Org. Biomol. Chem., 2010, 8, 4066
    DOI: 10.1039/C0OB00182A

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