3P079 抗菌ペプチド cecropin P1 の大腸菌発現系における発現効率 に影響を与える要因の解明 Elucidation of influential factor for productivity of the antimicrobial peptide using Escherichia coli

Cecropin P1 (CP1), an antimicrobial peptide found in nematodes from the stomachs of pigs, is 31 amino acids in length. In a membrane-like environment, CP1 forms an α-helical structure and believed to damage microbial membranes. We designed a soluble fusion protein that contains thioredoxin on the N-terminal side of CP1. This fusion construct still showed the cytotoxicity upon the expression in the Escherichia coli cells. However, this toxic behavior was improved when we tried the expression of the derivatives lacking a few C-terminal residues. In this study, we focused on the C-terminal region of CP1 and investigated the contribution of this region to the inhibition of E. coli growth and to the interaction with E. coli membranes using some fluorescent dyes.