摘要
首次设计开发一种促愈合,抗细菌感染的多肽分子——人源抗菌肽LL-37修饰haFGF的融合蛋白,旨在探讨此新型融合蛋白LL-37-haFGF的复性及纯化条件。利用重组大肠杆菌表达LL-37-haFGF并鉴定,初步考察8种复性添加小分子对其包涵体复性的作用,经分析表明,添加0.3 mol/L精氨酸可以大大提高LL-37-haFGF的复性效率。经镍亲和色谱及CM阳离子色谱纯化获得纯品。本研究获得了5.9 mg纯度为95.43%的LL-37-haFGF目的蛋白,为研究其功能奠定了基础,也为类似的双功能多肽的制备提供了参考依据。
A new multifunctional healing peptide was designed and developed for the first time, human antimicrobial peptide LL-37 modified haFGF fusion proteins, which can promote healing and fight infection. This paper discussed renaturation conditions and purification conditions of the new fusion protein named recombinant LL-37-haFGF was expressed by Escherichia coli and identified of effects on the refolding of eight kinds of small molecules added to inclusion bodies were preliminary investigated. The result showed supplementation of 0.3 mol/L arginine can greatly improve renaturation efficiency of LL-37-haFGF. The pure product of was obtained with nickel affinity chromatography and CM cation chromatography. Through this study, we obtained 5.9 mg target protein of high purity 95.43%, laying the function for its functional study, and also providing the reference for the preparation of similar multifunctional polypeptide.
出处
《生物技术通报》
CAS
CSCD
北大核心
2013年第4期210-214,共5页
Biotechnology Bulletin
基金
广州市科技支撑计划项目(2010J-E411)
广东省教育厅育苗计划(LYM11082)
