本研究通过同源建模方法，模拟结核分枝杆菌H37Rv来源的吲哚-­3­-甘油磷酸合成酶(IGPS)的结构，采用分子对接法，以IGPS结构为基础，从包含60 000种化合物的Maybridge化合物库中筛选出能与IGPS活性中心良好结合的化合物，并用抑菌实验等生物学方法进行验证。结果表明，化合物ATB26能与IGPS很好结合，且能体外有效抑制H37Rv和临床分离的敏感和耐药菌株的生长，其对结核分枝杆菌的体外最低抑菌浓度约为0.1 μg/ml。细胞毒性实验表明，ATB26与临床常用抗结核药物异烟肼、乙胺丁醇类似，对THP­1细胞系毒性较小。结果提示，化合物ATB26是一个新型IGPS抑制剂，有望开发成为新型的抗结核药，也可作为新型抗结核药物开发的一个潜在靶点。

In this study, the structure of indole-3-glycerol phosphate synthase (IGPS) from Mycobacterium tuberculosis (M. tuberculosis) H37Rv was obtained by homologous modeling. Based on the IGPS structure, virtual screening was carried out to select novel inhibitors  from  the Maybridge database with about sixty thousands organic compounds. Through biological selection, one compound, named ATB26, was identified as a potential inhibitor of IGPS, which showed potent antimycobacterial activity not only against M. tuberculosis H37Rv, but also against clinical isolates of multidrug-resistant M. tuberculosis strains with (minimal inhibition concentration, MIC) of 0.1 μg/ml. ATB26 could bound tightly to IGPS in vitro and obviously inhibited activity of IGPS. These results suggest that ATB26 is a novel potent inhibit of IGPS, and that IGPS might be a potential target for the development of new anti-tuberculosis drugs.