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耐甲氧西林金黄色葡萄球菌 FemB 蛋白的克隆、纯化及生物物理特性分析与抑制剂筛选。

Cloning, Purification, and Biophysical Characterization of FemB Protein from Methicillin-Resistant Staphylococcus aureus and Inhibitors Screening.

机构信息

Molecular Medicine Lab, Dept. of Genetics & Biotechnology, Osmania University, Hyderabad, Telangana, 500007, India.

Department of Chemistry, Nizam College, Osmania University, Hyderabad, Telangana, 500001, India.

出版信息

Appl Biochem Biotechnol. 2024 Aug;196(8):4974-4992. doi: 10.1007/s12010-023-04780-8. Epub 2023 Nov 22.

DOI:10.1007/s12010-023-04780-8
PMID:37991634
Abstract

Methicillin-resistant Staphylococcus aureus has emerged as a leading cause of nosocomial, community acquired infections worldwide. Earlier investigations revealed that mecA-encoded FEM proteins play a role in antimicrobial resistance by developing unique peptidoglycan cross-linking which helps in the formation of protective cell membrane. In view to this, present study focused on expression, purification FEM proteins, and FemB biophysical characterization with the aid of in silico and in vitro approaches. Furthermore, we carried out biological screening assays and identified the novel potent 1,2,3-triazole conjugated 1,3,4-oxadiazole hybrid molecule which could inhibit the MRSA than the proven oxacillin.

摘要

耐甲氧西林金黄色葡萄球菌已成为全球医院获得性和社区获得性感染的主要原因。早期的研究表明,mecA 编码的 FEM 蛋白通过形成独特的肽聚糖交联来发挥作用,从而有助于形成保护性细胞膜,从而在抗微生物药物耐药性中发挥作用。有鉴于此,本研究主要集中在表达、纯化 Fem 蛋白,并借助于计算机和体外方法对 FemB 进行生物物理特性分析。此外,我们还进行了生物筛选试验,鉴定出一种新型有效的 1,2,3-三唑偶联 1,3,4-噁二唑杂化分子,该分子对 MRSA 的抑制作用强于已证实的苯唑西林。

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