Expression analysis of an elastin-like polypeptide (ELP) in a cell-free protein synthesis system

被引:8
|
作者
Chu, Hun-Su [2 ]
Lee, Kyung-Ho [3 ]
Park, Ji-Eun [1 ]
Kim, Dong-Myung [3 ,4 ]
Kim, Byung-Gee [2 ,5 ]
Won, Jong-In [1 ]
机构
[1] Hongik Univ, Dept Chem Engn, Seoul 121791, South Korea
[2] Seoul Natl Univ, Sch Chem & Biol Engn, Seoul 151742, South Korea
[3] Chungnam Natl Univ, Interdisciplinary Program Nanotechnol, Taejon 305764, South Korea
[4] Chungnam Natl Univ, Dept Fine Chem Engn & Appl Chem, Taejon 305764, South Korea
[5] Seoul Natl Univ, Interdisciplinary Program Biochem Engn & Biotechn, Seoul 151742, South Korea
关键词
Cell-free protein synthesis; Elastin-like polypeptide (ELP); Protein expression profile; Recursive directional ligation (RDL) method; Repetitive polypeptides; RECOMBINANT PROTEINS; ESCHERICHIA-COLI; CTG REPEATS; PURIFICATION; CLONING;
D O I
10.1016/j.enzmictec.2009.10.003
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
An elastin-like polypeptide (ELP) fusion protein was expressed in a cell-free protein synthesis system, and the expression profile was analyzed quantitatively. By selective addition of specific amino acids constituting ELP molecules, the expression level of the ELP fusion protein was improved by 1.3-1.8 times as high as positive control. This result implies that the expression amount of long repetitive polypeptides, which was dramatically decreased in vivo system, can be compensated to a degree by adding repeatedly consumed amino acids in vitro system. Presented results demonstrate the potential of cell-free protein synthesis for high-throughput study of various repetitive polypeptides. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:87 / 91
页数:5
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