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来自巴西利什曼原虫的羊毛甾醇14-α-脱甲基酶(LbCYP51)的克隆、表达、纯化及分光光度分析

Cloning, expression, purification and spectrophotometric analysis of lanosterol 14-alpha demethylase from Leishmania braziliensis (LbCYP51).

作者信息

Freitas Humberto F, Leal Pires Acássia Benjamim, Castilho Marcelo S

机构信息

Faculdade de Farmácia, Universidade Federal da Bahia, Salvador, BA, 40170-290, Brazil.

Programa de pós-graduação em Biotecnologia, Universidade Estadual de Feira de Santana, Feira de Santana, BA, Brazil.

出版信息

Mol Biol Rep. 2018 Apr;45(2):175-183. doi: 10.1007/s11033-018-4150-7. Epub 2018 Jan 23.

Abstract

Leishmaniasis, a neglected tropical disease, is a major cause of morbidity and mortality worldwide. Of the three main clinical forms, cutaneous leishmaniasis (CL) is the most common and 40 million people are at risk in the endemic areas. Currently, the available drugs to fight leishmaniasis have high toxicity and poor efficiency. Then, it is very important to search for effective and safe drugs that would target essential enzymes from the parasite, such as lanosterol 14-alpha demethylase (CYP51, EC 1.14.13.70) from Leishmania braziliensis. Because most drug design efforts have been directed for Leishmania non-braziliensis species, there is no structural or kinetic data regarding L. braziliensis CYP51. Herein, we present for the first time molecular biology efforts and purification protocol to obtain the enzyme LbCYP51. These results lay the ground for future investigation of drugs against this target.

摘要

利什曼病是一种被忽视的热带疾病,是全球发病和死亡的主要原因。在三种主要临床类型中,皮肤利什曼病(CL)最为常见,流行地区有4000万人面临风险。目前,用于治疗利什曼病的现有药物毒性高且效率低。因此,寻找针对该寄生虫关键酶的有效且安全的药物非常重要,例如来自巴西利什曼原虫的羊毛甾醇14-α脱甲基酶(CYP51,EC 1.14.13.70)。由于大多数药物设计工作都针对非巴西利什曼原虫物种,因此尚无关于巴西利什曼原虫CYP51的结构或动力学数据。在此,我们首次展示了获得LbCYP51酶的分子生物学研究和纯化方案。这些结果为未来针对该靶点的药物研究奠定了基础。

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