Cloning And Fusion Expression Of Antibactorial Peptide Cecropin X In Escherichia Coli

Background & Objective The increasing problem of traditional antibiotic resistance among pathogenic bacteria requires development of new antimicrobial agents. Antibiotics peptides are a new group of antimicrobial peptide .They are widely exist in natural and have been found in animal, plants, insects, and homo-sapiens. They form the first line of host defense against pathogenic infections and are a key component of the ancient innate immune system. They have a unique mechanism of bacterial action which make it can overcome the growing problems of antibiotic resistance. Cecropin family is one kind of the initial found antibiotics peptides. Several Studies have shown that Cecropin have an effect on bacteria, fungi, viruses and cancer cells. All of the beneficial physiological activities make it an obvious choice to substitute with traditional antibiotics. In this reseach, we want to construct the prokaryotic expression plasmid of Cecropin X gene and express fusion protein. And then determining its antibacterial activity. The aim of the present investigation was to find a more strong antimicrobial peptide by gene recombinant technology. Methods Based on the amino acid sequence of native antibiotics peptides originated from Heliothis virescens, we designed the amino acid sequence of Cecropin X. The Cecropin X gene transformed was synthesized chemically and inserted into fusion expression vector pGEX-5X-3. Recombinant plasmid was transformed into E.coli BL21 and fusion protein...