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A novel expression vector for the improved solubility of recombinant scorpion venom in Escherichia coli.

Abstract：

:Recombinant scorpion anti-excitation peptide (rANEP) has previously been expressed using the pET32a system and purified via affinity chromatography. However, rANEP is expressed in BL21(DE3) cells as an inclusion body, and the affinity tag can not be removed. To overcome this problem, we used a variety of protein, DsbA, MBP, TrxA, intein, and affinity tags in fusion and co-expression to achieve soluble and functional rANEP without any affinity tag. In the pCIT-ANEP expression vector, the highest soluble expression level was approximately 90% of the total cellular proteins in E. coli, and the rANEP was cleaved by the intein protein and subsequently purified to obtain rANEP, which had the same activity as the natural ANEP. The purity of rANEP obtained using this method was over 95%, with a quantity of 5.1 mg from of purified rANEP from 1 L of culture. This method could expand the application of the soluble expression of disulfide-rich peptides in E. coli.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Han T,Ming H,Deng L,Zhu H,Liu Z,Zhang J,Song Y

doi

10.1016/j.bbrc.2016.09.047

subject

Has Abstract

pub_date

2017-01-01 00:00:00

pages

120-125

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(16)31498-X

journal_volume

482

pub_type

杂志文章

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