Nonaromatic sulfonamide group as an ideal anchor for potent human carbonic anhydrase inhibitors: role of hydrogen-bonding networks in ligand binding and drug …
F Abbate, CT Supuran, A Scozzafava… - Journal of medicinal …, 2002 - ACS Publications
Journal of medicinal chemistry, 2002•ACS Publications
X-ray crystal structures of the adducts of human carbonic anhydrase (hCA) isozyme II with
derivatives incorporating a sulfamide or sulfamic acid moiety are reported. The absence of a
C− SO2NH2 bond in the first type of compound can be exploited for the design of more
potent and selective CA inhibitors. This study also explains why sulfate is a several-orders-of-
magnitude weaker CA inhibitor compared to derivatives incorporating
sulfonamide/sulfamide moieties.
derivatives incorporating a sulfamide or sulfamic acid moiety are reported. The absence of a
C− SO2NH2 bond in the first type of compound can be exploited for the design of more
potent and selective CA inhibitors. This study also explains why sulfate is a several-orders-of-
magnitude weaker CA inhibitor compared to derivatives incorporating
sulfonamide/sulfamide moieties.
X-ray crystal structures of the adducts of human carbonic anhydrase (hCA) isozyme II with derivatives incorporating a sulfamide or sulfamic acid moiety are reported. The absence of a C−SO2NH2 bond in the first type of compound can be exploited for the design of more potent and selective CA inhibitors. This study also explains why sulfate is a several-orders-of-magnitude weaker CA inhibitor compared to derivatives incorporating sulfonamide/sulfamide moieties.
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