Design and production of a novel antimicrobial fusion protein in Escherichia coli

摘要: In recent years, antimicrobial peptides (AMPs) have attracted increasing attention. The microbial cells provide a simple, cost-effective platform to produce AMPs in industrial quantities. While AMP production as fusion proteins microorganisms is commonly used, the recovery of necessitates use expensive proteases and extra purification steps. Here, we develop novel protein DAMP4-F-pexiganan comprising carrier DAMP4 linked AMP, pexiganan, through long, flexible linker. We show that this can be purified using non-chromatography approach exhibits same activity chemically synthesized pexiganan peptide without any cleavage step. Activity dependent on linker between domains, well expression conditions protein, with low-temperature promoting better folding domain. circumvents time-consuming costly steps chromatography-based enzymatic cleavages, therefore shows considerable advantages over traditional AMPs. expect studies effect its activity, will broaden rational design products based