high-yield soluble expression and simple purification of the antimicrobial peptide og2 using the intein system in escherichia coli
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2013
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Abstract
OG2 is a modified antimicrobial peptide, that is, derived from the frog peptide Palustrin-OG1. It has high antimicrobial activity and low cytotoxicity, and it is therefore promising as a therapeutic agent. Both prokaryotic (Escherichia coli) and eukaryotic (Pichia pastoris) production host systems were used to produce OG2 in our previous study; however, it was difficult to achieve high expression yields and efficient purification. In this study, we achieved high-yield OG2 expression using the intein fusion system. The optimized OG2 gene was cloned into the pTWIN1 vector to generate pTWIN-OG2-intein2 (C-terminal fusion vector) and pTWIN-intein1-OG2 (N-terminal fusion vector). Nearly 70% of the expressed OG2-intein2 was soluble after the IPTG concentration and induction temperature were decreased, whereas only 42% of the expressed of intein1-OG2 was soluble. Up to 75 mg of OG2-intein2 was obtained from a 1 l culture, and 85% of the protein was cleaved by 100 mM DTT. Intein1-OG2 was less amenable to cleavage due to the inhibition of cleavage by the N-terminal amino acid of OG2. The purified OG2 exhibited strong antimicrobial activity against E. coli K88. The intein system is the best currently available system for the cost-effective production of OG2.
| Reference Key |
xie2013biomedhigh-yield
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|---|---|
| Authors | ;Yong-Gang Xie;Fei-Fei Han;Chao Luan;Hai-Wen Zhang;Jie Feng;Young-Jun Choi;Denis Groleau;Yi-Zhen Wang |
| Journal | spectrochimica acta - part a: molecular and biomolecular spectroscopy |
| Year | 2013 |
| DOI |
10.1155/2013/754319
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| URL | |
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