Abstract
We have synthesized alrestatin derivatives 1–11 possessing acyl benzenesulfonamide groups as surrogates for the carboxylic acid moiety of alrestatin. Most of the compounds were inactive as aldose reductase inhibitors compared to alrestatin, however, some of them demonstrated selectivity towards inhibition of rat kidney aldehyde reductase compared to rat lens aldose reductase suggesting that structural differences may exist between the carboxylic acid binding domains of these closely related enzymes. The chemoreactive derivatives 9 and 10 suggested the presence of a nucleophile(s) at the carboxylic acid binding site on aldose reductase.
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