Purification of recombinant proteins by fusion with thermally-responsive polypeptides

被引:719
作者
Meyer, DE [1 ]
Chilkoti, A [1 ]
机构
[1] Duke Univ, Dept Biomed Engn, Durham, NC 27708 USA
关键词
elastin-like polypeptide; inverse phase transition; environmentally responsive; fusion protein; protein purification;
D O I
10.1038/15100
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Elastin-like polypeptides (ELPs) undergo a reversible, inverse phase transition. Below their transition temperature (T-t), ELPs are soluble in water, but when the temperature is raised above ft, phase transition occurs, leading to aggregation of the polypeptide. We demonstrate a method for purification of soluble fusion proteins incorporating an ELF tag. Advantages of this method, termed "inverse transition cycling," include technical simplicity, low cost, ease of scale-up, and capacity for multiplexing. More broadly, the ability to environmentally modulate the physicochemical properties of recombinant proteins by fusion with ELPs will allow diverse applications in bioseparation, immunoassays, biocatalysis, and drug delivery.
引用
收藏
页码:1112 / 1115
页数:4
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