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Acylsulfonamide-containing PTP1B inhibitors designed to mimic an enzyme-bound water of hydration

  1. Author:
    Liu, D. G.
    Gao, Y.
    Voigt, J. H.
    Lee, K.
    Nicklaus, M. C.
    Wu, L.
    Zhang, Z. Y.
    Burke, T. R.

  2. Author Address

    NCI Frederick, CCR, Lab Med Chem, NIH, Ft Detrick, MD 21702 USA NCI Frederick, CCR, Lab Med Chem, NIH, Ft Detrick, MD 21702 USA Albert Einstein Coll Med, Dept Mol Pharmacol, Bronx, NY 10461 USA Burke TR NCI Frederick, CCR, Lab Med Chem, NIH, Ft Detrick, MD 21702 USA
    1. Year: 2003
  2. Journal: Bioorganic & Medicinal Chemistry Letters
    1. 13
    2. 18
    3. Pages: 3005-3007
  4. Type of Article: Article
  1. Abstract:

    Previously, it had been reported that 6- (phosphonodifluoromethyl)-2-naphthoic acid binds to the protein-tyrosine phosphatase PTP1B with its 2-carboxyl group interacting only indirectly through a bridging water molecule. Reported herein is a family of new analogues that utilize acylsulfonamido functionality both to mimic this water of hydration and to provide an additional new site for elaboration not found in the parent carboxyl-containing analogue. Target acylsulfonamides were prepared in two steps from commercially available primary sulfonamides, which were selected based on in silico screening for their potential ability to interact with one of three binding surfaces proximal to the PTP1B catalytic site. In general, modest potency enhancements were observed. Arylacylsulfonamides represent a structure-based extension of inhibitor design that may have broader utility in the development of PTP1B inhibitors. (C) 2003 Elsevier Ltd. All rights reserved.

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