Production of antimicrobial peptide (Oxysterlin 1) in Escherichia coli with ELP self-cleavage tag / 生物工程学报
Chinese Journal of Biotechnology
; (12): 2915-2923, 2021.
Article
em Zh
| WPRIM
| ID: wpr-887853
Biblioteca responsável:
WPRO
ABSTRACT
Antimicrobial peptides are the most promising alternatives to antibiotics. However, the strategy of producing antimicrobial peptides by recombinant technology is complicated and expensive, which is not conducive to the large-scale production. Oxysterlin 1 is a novel type of cecropin antimicrobial peptide mainly targeting on Gram-negative bacteria and is of low cytotoxicity. In this study, a simple and cost-effective method was developed to produce Oxysterlin 1 in Escherichia coli. The Oxysterlin 1 gene was cloned into a plasmid containing elastin-like polypeptide (ELP) and protein splicing elements (intein) to construct the recombinant expression plasmid (pET-ELP-I-Oxysterlin 1). The recombinant protein was mainly expressed in soluble form in E. coli, and then the target peptide can be purified with a simple salting out method followed by pH changing. The final yield of Oxysterlin 1 was about 1.2 mg/L, and the subsequent antimicrobial experiment showed the expected antimicrobial activity. This study holds promise for large-scale production of antimicrobial peptides and the in-depth study of its antimicrobial mechanism.
Palavras-chave
Texto completo:
1
Índice:
WPRIM
Assunto principal:
Peptídeos
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Proteínas Recombinantes de Fusão
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Elastina
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Inteínas
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Escherichia coli
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Proteínas Citotóxicas Formadoras de Poros
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2021
Tipo de documento:
Article