Abbate Francesco, Casini Angela, Owa Takashi, Scozzafava Andrea, Supuran Claudiu T
Università degli Studi di Firenze, Polo Scientifico, Dipartimento di Chimica, Laboratorio di Chimica Bioinorganica, Via della Lastruccia 3, Rm. 188, I-50019 Sesto Fiorentino, Florence, Italy.
Bioorg Med Chem Lett. 2004 Jan 5;14(1):217-23. doi: 10.1016/j.bmcl.2003.09.062.
E7070 [N-(3-chloro-7-indolyl)-1,4-benzenedisulfonamide] is an anticancer drug candidate under clinical development for the treatment of several types of cancers. We prove here that this compound also acts as a potent carbonic anhydrase (CA) inhibitor. Similarly to the clinically used drugs acetazolamide, methazolamide and topiramate, E7070 showed inhibition constants in the range of 15-31nM against isozymes I, II and IX, being slightly less effective as a CA IV inhibitor (K(i) of 65nM). The X-ray crystal structure of the adduct of hCA II with E7070 revealed unprecedented interactions between the inhibitor and the active site, with three different conformations of the chloroindole fragment of the inhibitor interacting with different amino acid residues/water molecules of the enzyme. A superimposition of these conformations with those of other sulfonamide/sulfamate CA inhibitors indicated that similar regions of the hCA II active site could be involved in the interaction with inhibitors.
E7070 [N-(3-氯-7-吲哚基)-1,4-苯二磺酰胺] 是一种正处于临床开发阶段的抗癌候选药物,用于治疗多种类型的癌症。我们在此证明,该化合物还可作为一种有效的碳酸酐酶(CA)抑制剂。与临床使用的药物乙酰唑胺、甲醋唑胺和托吡酯类似,E7070对同工酶I、II和IX的抑制常数在15 - 31 nM范围内,作为CA IV抑制剂的效果稍差(K(i)为65 nM)。hCA II与E7070加合物的X射线晶体结构揭示了抑制剂与活性位点之间前所未有的相互作用,抑制剂的氯吲哚片段有三种不同构象与酶的不同氨基酸残基/水分子相互作用。将这些构象与其他磺酰胺/氨基磺酸盐CA抑制剂的构象进行叠加表明,hCA II活性位点的相似区域可能参与与抑制剂的相互作用。