a Programa de pós-graduação em Biotecnologia , Universidade Estadual de Feira de Santana , Feira de Santana , BA , Brazil.
b Departamento de Antibióticos, Universidade Federal de Pernambuco, Recife, PE, Brazil.
J Enzyme Inhib Med Chem. 2019 Dec;34(1):333-342. doi: 10.1080/14756366.2018.1550752.
Leishmaniasis is considered as one of the major neglected tropical diseases due to its magnitude and wide geographic distribution. Leishmania braziliensis, responsible for cutaneous leishmaniasis, is the most prevalent species in Brazil. Superoxide dismutase (SOD) belongs to the antioxidant pathway of the parasites and human host. Despite the differences between SOD of Leishmania braziliensis and human make this enzyme a promising target for drug development efforts. No medicinal chemistry effort has been made to identify LbSOD inhibitors. Herein, we show that thermal shift assays (TSA) and fluorescent protein-labeled assays (FPLA) can be employed as primary and secondary screens to achieve this goal. Moreover, we show that thiazole derivatives bind to LbSOD with micromolar affinity.
利什曼病由于其规模和广泛的地理分布,被认为是主要的被忽视热带病之一。引起皮肤利什曼病的巴西利什曼原虫是在巴西最为普遍的物种。超氧化物歧化酶(SOD)属于寄生虫和人体宿主的抗氧化途径。尽管巴西利什曼原虫的 SOD 与人 SOD 之间存在差异,但该酶仍然是药物开发的一个很有前途的靶点。尚未有药物化学方面的努力来鉴定 LbSOD 抑制剂。在此,我们表明,热转移测定(TSA)和荧光蛋白标记测定(FPLA)可作为初步和二次筛选来实现这一目标。此外,我们还表明噻唑衍生物与 LbSOD 以微摩尔亲和力结合。