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首页> 外文期刊>Current Microbiology: An International Journal >Expression and Purification of an Antimicrobial Peptide, Bovine Lactoferricin Derivative LfcinB-W10 in Escherichia coli
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Expression and Purification of an Antimicrobial Peptide, Bovine Lactoferricin Derivative LfcinB-W10 in Escherichia coli

机译：抗菌肽牛乳铁蛋白衍生物LfcinB-W10在大肠杆菌中的表达和纯化

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摘要

Antimicrobial peptides (AMPs) are extremely attractive candidate for therapeutic agents due to their wide spectrum of antimicrobial activity and action mechanism different from antibiotics. In this study, a method using genetic engineering for obtaining an antimicrobial peptide, bovine lactoferricin derivative peptide LfcinB-W10, has been developed. According to the coden usage of Escherichia coli, a gene encoding the peptide was synthesized and a recombinant vector of E. coli expression pGEX-EN-LFW was constructed. The LfcinB-W10 peptide fused with glutathione S-transferase (GST) was successfully expressed and about 20 mg fusion protein with 90% purity was obtained from 1 l culture. The recombinant LfcinB-W10 (rLfcinB-W10) was released from fusion protein by the enterokinase digestion, and about the LfcinB-W10 yield reached 300 og per 1 l culture. The purified rLfcinB-W10 was found to have growth inhibition activity against Staphylococcus aureus (S. aureus) ATCC25923.
机译：抗菌肽（AMPs）具有广泛的抗菌活性和不同于抗生素的作用机理，因此成为治疗剂的极具吸引力的候选者。在这项研究中，已开发出一种利用基因工程技术获得抗菌肽牛乳铁蛋白衍生物肽LfcinB-W10的方法。根据大肠杆菌的编码用法，合成了编码该肽的基因，并构建了大肠杆菌表达pGEX-EN-LFW的重组载体。与谷胱甘肽S-转移酶（GST）融合的LfcinB-W10肽成功表达，并从1μl培养物中获得了约20 mg纯度为90％的融合蛋白。通过肠激酶消化，重组LfcinB-W10（rLfcinB-W10）从融合蛋白中释放出来，每1升培养液约产生300 og LfcinB-W10产量。发现纯化的rLfcinB-W10对金黄色葡萄球菌（金黄色葡萄球菌）ATCC25923具有生长抑制活性。

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