A Novel hybrid peptide Cecropin A(1-8)-LL37(17-30) with great Antibacterial Activity

• 作 者: Xubiao Wei Dayong Si Zhaojun Zheng Lulu Zhang Rujuan Wu Rijun Zhang
• 机 构: Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Scienc
• 出 处: 中国畜牧兽医学会动物微生态学分会第五届第十二次全国学术研讨会
• 发表日期: 2016年12期
• 关键词: hybrid peptide Cecropin A(1-8)-LL-37(17-30) antibacterial activity hemolytic act

　　Antimicrobial peptides are attracting more attention as a therapeutic alternative compared to traditional antibiotics in the field of disease control and prevention due to their unique mechanism of action and broad spectrum antimicrobial activity.LL-37 (L), a linear helical peptide isolated from human leukocytes and epithelia, plays a critical role in the process of antimicrobial infection, angiogenesis,wound healing and apoptosis[1].However, it shows undesirable hemolytic activity against eukaryotic cells by inducing membrane disruption, which largely limits its application in clinic[2].Cecropin A (C),a antibacterial peptide produced by Hyalophora cecropia, shows broad bioactivities such as antibacterial,anti-inflammation and anticancer, but it does not lyses eukaryotic cells[3, 4].In our study, the hybrid peptide C(1-8)-L(17-30) (C-L) was designed by combining the N-terminal amphipathic α-helix fragment of C with the core antimicrobial fragment of L on the basis of the hypothesis that the combination will elevate the antimicrobial property and minimize the hemolytic activity.Results showed that the antibacterial property of C-L was greatly improved when compared to parental peptides, and C-L did not show cytotoxicity in comparison with L.Moreover, C-L was better than C and L in sterilization speed and efficacy.In sum, this research not only supplied an effective approach for acquiring excellent hybrid peptide C-L, but pave the way for its further exploration on pharmaceutical and medical importance.