抗菌肽在大肠杆菌中的融合表达  

Fusion expression of antimicrobial peptides in Escherichia coli

作　　者：张学敏[1] 金莉莉[1] 王铮[1] 王秋雨[1] 

机构地区：[1]辽宁大学生命科学院,辽宁沈阳110036

出　　处：《生物工程学报》2014年第8期1172-1181,共10页Chinese Journal of Biotechnology

基　　金：国家自然科学基金(No.31071916);沈阳市科技计划项目(No.F12-277-1-40)资助~~

摘　　要：抗菌肽作为新一代抗生素的潜在应用价值使其备受关注,大量高纯度的抗菌肽是开展基础及临床实验的关键。天然来源的抗菌肽资源有限、纯化困难,化学合成抗菌肽成本高、活性不稳定,因此通过基因重组表达得到大量抗菌肽是低成本、高效益的方法。目前采用大肠杆菌表达系统获得抗菌肽已成为研究者的首选,通常以形成融合蛋白的方式表达,这不仅可避免抗菌肽对宿主的杀伤作用,也保护了抗菌肽免受蛋白酶降解。文章结合课题组的研究工作,综述了近年来抗菌肽在大肠杆菌中表达的融合载体、融合蛋白的裂解方法及表达条件优化的研究进展。Due to their potential application as novel antibiotics, antimicrobial peptides are attracting much attention. Large quantities of highly purified peptides are crucial to basic and clinical studies. Natural resources of antimicrobial peptides are limited and hard to purify, chemical synthesis is of high-cost and unstable, so recombinant expression of antimicrobial peptides is a cost-effective way. Escherichia coil has been the most widely used as host to expressantimicrobial peptides with fusion protein, which can not only avoid the lethal effect towards the host, but also protect the peptide from degradation by proteases. Combined with our research, the present article reviews the progress of fusion vector, cleavage methods and optimization options for antimicrobial peptides production with fusion protein in Escherichia coil.

关 键 词：抗菌肽 载体蛋白 融合表达 裂解方法 条件优化 

分 类 号：Q78[生物学—分子生物学]