期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 45, 期 17, 页码 3583-3587出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm011131t
关键词
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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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