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Recombinant expression, purification, and antimicrobial activity of a novel hybrid antimicrobial peptide LFT33

文献类型： 外文期刊

作者： Feng, Xingjun 1 ; Liu, Chunlong 2 ; Guo, Jiayin 1 ; Song, Xueying 1 ; Li, Jing 1 ; Xu, Wenshan 1 ; Li, Zhongqiu 3 ;

作者机构： 1.NE Agr Univ, Coll Anim Sci & Technol, Harbin 150030, Peoples R China

2.Chinese Acad Sci, NE Inst Geog & Agroecol, Key Lab Mollisols Agroecol, Harbin 150081, Peoples R China

3.Heilongjiang Acad Agr Sci, Anim Husb Res Ctr, Harbin 150086, Peoples R China

关键词： Antimicrobial peptides;Hybrid peptides;LfcinB;Thanatin;Prokaryotic expression

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：4.813； 五年影响因子：4.697 ）

ISSN： 0175-7598

年卷期： 2012 年 95 卷 5 期

页码：

收录情况： SCI

摘要： With great therapeutic potential against antibiotic-resistant bacteria, viruses, and even parasites, antimicrobial peptides (AMPs) have received increased interest as pharmaceutical agents in recent years. It is a worthy yet challenging work to carry out the implement and improvement of AMPs production using bioengineering techniques. In the present study, a novel hybrid peptide LFT33 was designed derived from LfcinB and thanatin. The cDNA fragment encoding LFT33 with preferred codons of Escherichia coli was chemically synthesized and ligated into the vector pET32a(+) to express the LFT33 fusion protein. The fusion protein was successfully expressed in soluble form in E. coli induced under optimized conditions. After purification by affinity chromatography, the fusion protein was cleaved successfully by enterokinase and released the peptide LFT33. About 0.5 mg of the recombinant LFT33 was obtained by reversed-phase high performance liquid chromatography from 1 l of culture medium. Mass spectrometry analysis of the purified recombinant LFT33 demonstrated that the molecular weight perfectly matched the calculated mass (4,195 Da). The recombinant peptide LFT33 caused an increase in antimicrobial activity (IC50 = 16-64 mu g/ml) against given strains and did not show hemolytic activity for human erythrocytes. The results indicated that the hybrid peptide LFT33 could serve as a promising candidate for pharmaceutical agents.

  • 相关文献

[1]Design and high-level expression of a hybrid antimicrobial peptide LF15-CA8 in Escherichia coli. Feng, Xing-Jun,Xing, Li-Wei,Liu, Di,Song, Xue-Ying,Li, Jing,Xu, Wen-Shan,Liu, Chun-Long,Li, Zhong-Qiu. 2014

[2]High-Yield Recombinant Expression of the Chicken Antimicrobial Peptide Fowlicidin-2 in Escherichia coli. Feng, Xingjun,Xu, Wenshan,Qu, Pei,Li, Xiaochong,Xing, Liwei,Liu, Di,Jiao, Jian,Wang, Jue,Li, Zhongqiu,Liu, Chunlong,Liu, Chunlong.

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