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首页> 外文期刊>Biochemistry >Molecular Basis for the Origin of Differential Spectral and Binding Profiles of Dansylamide with Human Carbonic Anhydrase I and II
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Molecular Basis for the Origin of Differential Spectral and Binding Profiles of Dansylamide with Human Carbonic Anhydrase I and II

机译：丹磺酰胺与人碳酸酐酶I和II的光谱和结合谱的起源的分子基础

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摘要

Sulfonamide derivatives serve as potent inhibitors of carbonic anhydrases(CAs),and a few such inhibitors have been currently used as drugs for the treatment of different pathogenic conditions in humans.In pursuit of designing the isozyme-specific inhibitors of human CAs,we observed that the fluorescence spectral properties and binding profiles of a fluorogenic sulfonamide derivative,5-(di-methylamino)-l-naphthalenesulfonamide(dansylamide,DNS A),were markedly different between the recombinant forms of human carbonic anhydrase I(hCA I)and II(hCA II).The kinetic evaluation of the overall microscopic pathways for the binding of DNSA to hCA I versus hCA II revealed that the protein isomerization step served as a major determinant of the above discrepancy.Arguments are presented that the detailed structural-functional investigations of enzyme-ligand interactions may provide insights into designing the isozyme-specific inhibitors of CAs.
机译：磺酰胺衍生物可作为有效的碳酸酐酶（CAs）抑制剂，目前已经有几种此类抑制剂被用作治疗人类不同病原性疾病的药物。在设计人CA的同工酶特异性抑制剂时，我们观察到：人源碳酸酐酶I（hCA I）和II（II）的重组形式的荧光磺酰胺衍生物5-（二甲基氨基）-1-萘磺酰胺（丹磺酰胺，DNS A）的荧光光谱性质和结合特性DNSA与hCA I相对于hCA II结合的整体微观途径的动力学评估表明，蛋白质异构化步骤是上述差异的主要决定因素。酶与配体的相互作用可能为设计CA的同工酶特异性抑制剂提供了见识。

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