TY - JOUR
T1 - The interaction of anhydroalditols with sweet-almond β-glucosidase and Escherichia coli β-galactosidase: Implications for the design of potent glycosidase inhibitors
AU - Field, Robert A.
AU - Haines, Alan H.
AU - Chrystal, Ewan J. T.
N1 - Funding Information:
Science and Engineering Research Council and
PY - 1991
Y1 - 1991
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0026315306&partnerID=8YFLogxK
U2 - 10.1016/S0960-894X(01)81044-1
DO - 10.1016/S0960-894X(01)81044-1
M3 - Article
AN - SCOPUS:0026315306
SN - 0960-894X
VL - 1
SP - 667
EP - 672
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
IS - 12
ER -