牛乳铁蛋白素-马盖宁杂合抗菌肽的设计、合成及抑菌活性

摘要

根据抗菌肽牛乳铁蛋白素(Lfcin B)与马盖宁(Magainin)的核心功能序列,将Lfcin B(1-15)和Magainin(1-12)二者连接起来,设计一种新型杂合抗菌肽LFB15-MA12,采用固相化学合成法合成获得纯度大于95%的LFB15-MA12.微量肉汤稀释法测得LFB15-MA12对金黄色葡萄球菌ATCC25923、大肠杆菌ATCC25922、绿脓杆菌ATCC27853、鼠伤寒沙门氏菌C77-31四种细菌的最小抑菌浓度(Minimal inhibition concentration,MIC)分别为16、64、64和32μg.mL-1,在抑菌浓度范围内未表现出溶血活性.获得了一种具有较高抗菌活性且安全无毒的新型抗菌肽,为研究开发理想的新型抗菌肽分子提供了新思路.%A novel hybrid antimicrobial peptide, LFB15-MA12, derived from the core function sequence of LfcinB and Magainin, was designed by connection between Lfcin B (1-15) and Magainin (1-12). The peptide LFB15-MA12 with purity above 95％ was obtained by solid phase synthesis of chemical method. The antimicrobial activity of the peptide was determined by small quantity broth microdilution method and MIC for S. aureus ATCC25923, E. coli ATCC25922, P. aeruginosa ATCC 27853 and S. typhimurium C77-31 was 16, 64, 64 and 32 μg. mL-1, respectively. The hemolytic activity was not observed for the peptide at the range of inhibitory concentration. A novel antimicrobial peptide, with improved antibacterial activity and property of safety and nontoxicity was obtained. This study provided a new method for research and development of novel antimicrobial peptides with ideal activities.