THE INTERACTION OF ANHYDROALDITOLS WITH SWEET-ALMOND BETA-GLUCOSIDASE AND ESCHERICHIA-COLI BETA-GALACTOSIDASE - IMPLICATIONS FOR THE DESIGN OF POTENT GLYCOSIDASE INHIBITORS
被引:11
作者:
FIELD, RA
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机构:UNIV E ANGLIA,SCH CHEM SCI,NORWICH NR4 7TJ,NORFOLK,ENGLAND
FIELD, RA
HAINES, AH
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机构:UNIV E ANGLIA,SCH CHEM SCI,NORWICH NR4 7TJ,NORFOLK,ENGLAND
HAINES, AH
CHRYSTAL, EJT
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机构:UNIV E ANGLIA,SCH CHEM SCI,NORWICH NR4 7TJ,NORFOLK,ENGLAND
CHRYSTAL, EJT
机构:
[1] UNIV E ANGLIA,SCH CHEM SCI,NORWICH NR4 7TJ,NORFOLK,ENGLAND
[2] ICI PLC,JEALOTTS HILL RES STN,BRACKNELL RG12 6EY,BERKS,ENGLAND
A range of 1,4- and 1,5-anhydroalditols have been synthesized and assessed for their ability to inhibit glycosidases. Observed inhibition indicates that aglycone-enzyme interactions contribute significantly to both the affinity and the stereoselectivity of substrate binding. Such interactions may also contribute to enzyme-transition state interactions. Implications for the design of potent glycosidase inhibitors are discussed.