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ABSTRACT: Background
Cecropin A (CeA), a natural cationic antimicrobial peptide, exerts potent antimicrobial activity against a broad spectrum of Gram-positive and Gram-negative bacteria, making it an attractive candidate substitute for antimicrobials. However, the low production rate and cumbersome, expensive processes required for both its recombinant and chemical synthesis have seriously hindered the exploitation and application of CeA. Here, we utilized a short β-structured self-aggregating protein, ELK16, as a fusion partner of CeA, which allowed the efficient production of high-purity CeA antibacterial peptide with a simple inexpensive process.Results
In this study, three different approaches to the production of CeA peptide were investigated: an affinity tag (His-tag)-fused pr
SUBMITTER: Wang M
PROVIDER: S-EPMC6173929 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature