报告题目：抗菌肽chensinin-1b的抗菌活性及与细胞膜作用机制研究

报告人：董维兵，辽宁师范大学生命科学学院教授，博士生导师

时间：4月20日

地点：1号实验楼302会议室

In this study, chensinin-1b was designed by rearranging the amino acid sequence of its hydrophilic/polar residues on one face and its hydrophobic/nonpolar residues on the opposite face according to its helical diagram, and by replacing three Gly residues with three Trp residues. Introduction of Trp residues significantly promoted the binding of the peptide to the bacterial outer membrane and exerted bactericidal activity through cytoplasmic membrane damage. Chensinin-1b demonstrates higher antimicrobial activity and greater cell selectivity than its parent peptide, chensinin-1. The electrostatic interactions between chensinin-1b and lipopolysaccharide (LPS) may have facilitated the uptake of the peptide into Gram-negative cells and be also helpful to disrupt the bacterial cytoplasmic membrane, as evidenced by depolarisation of the membrane potential and leakage of calceins from the liposomes of Escherichia coli and Staphylococcus aureus. Chensinin-1b was also found to penetrate mouse skin and was also effective in vivo, as measured by hydroxyproline levels in a wound infection mouse model, and could therefore act as an anti-infective agent for wound healing.

个人简介：

董维兵，辽宁师范大学生命科学学院教授，博士生导师，辽宁省首批“兴辽英才计划”青年拔尖人才。2008年在大连理工大学精细化工国家重点实验室获博士学位。2008年-2013年先后在日本名古屋大学野依物质科学国际研究中心、美国加州大学戴维斯分校化学系和宾夕法尼亚州立大学化学系从事博士后研究。目前研究方向为多肽药物研发。迄今为止已发表SCI论文30余篇。目前主持国家自然科学基金面上项目1项及其他多项省级项目。