2. Author's Information
    R A Field
    School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, U.K.

    A H Haines
    School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, U.K.

    E J T Chrystal
    ICI Agrochemicals, Jealott`s Hill Research Station, Bracknell, RG12 6EY, Berks., U.K.

    M C Luszniak
    School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, U.K.
  3. Abstract
    This present study reports the ability of a range of derivatives of L-histidine, histamine and imidazole to act as inhibitors of sweet-almond ?-glucosidase, yeast alpha-glucosidase and Escherichia coli ?-galactosidase. The addition of a hydrophobic group to the basic imidazole nucleus greatly enhances binding to both the alpha- and ?-glucosidases. L-Histidine (beta-naphthylamide (Ki 17 microM) is a potent competitive inhibitor of sweet-almond ?-glucosidase as is omega-N-acetylhistamine (K1 35 microM), which inhibits the sweet-almond ?-glucosidase at least 700 times more strongly than either yeast alpha-glucosidase or Escherichia coli ?-galactosidase, and suggests potential for the development of selective reversible ?-glucosidase inhibitors. A range of hydrophobic omega-N-acylhistamines were synthesized and shown to be among the most potent inhibitors of sweet-almond ?-glucosidase reported to date.
    Keywords
    Histidines, histamines, imidazoles, glycosidase inhibitors
    DOI: 10.1042/bj2740885
    ADLID: 91133-v4
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  1. Keywords
    Histidines histamines imidazoles glycosidase inhibitors
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