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Pubmed ID :29099325
Publication Date : //

Functional expression, purification and antimicrobial activity of a novel antimicrobial peptide MLH in Escherichia coli.


In this study, a novel heterozygous antimicrobial peptide MLH was synthesized, expressed, purified and characterized. The peptide MLH was selected through bioinformatic analysis using musca domestica antimicrobial peptide (Cec-Med), human antimicrobial peptide LL-37 and helicobacter pylori antimicrobial peptide (Hp) as parent peptides. The target gene was synthesized by overlap extension PCR (SOE-PCR) and connected to the expression vector pET-32a (+), and the recombinant plasmid pET-32a-MLH was transformed to Escherichia coli for constructing pET-32a-MLH/BL21 (DE3). IPTG was used to induce protein expression and SDS-PAGE and Western-Blot were adopted to test the target protein. And fermentation condition was optimized to get the mass expression of the fusion protein. The Ni2+ affinity chromatographic column was used to purify. Active heterozygous peptide was obtained after renaturation. Finally, the activity of the heterozygous antimicrobial peptide was identified. The fusion peptide showed significant antimicrobial effect on both E. coli and Staphylococcus aureus.

Authors : Gong Guo-Li , Wei Yuan , Wang Zhong-Zhong ,

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