Expression and purification of antimicrobial peptide buforin IIb in Escherichia coli |
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| Authors: | Qi Wang Fenfen Zhu Yinqiang Xin Jia Liu Lan Luo Zhimin Yin |
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| Affiliation: | (1) Jiangsu Province Key Laboratory for Molecular and Medicine Biotechnology, College of Life Science, Nanjing Normal University, Nanjing, No. 1 Wenyuan Road, Nanjing, 210046, Jiangsu, People’s Republic of China;(2) State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, 210093, People’s Republic of China; |
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| Abstract: | A novel production method in Escherichia coli for an antimicrobial peptide of 21 amino acids, buforin IIb, which is a synthetic analog of buforin II, has been developed. The buforin IIb gene was cloned into the vector pET32a to construct an expression vector pET32a–buforin IIb. The fusion protein Trx-buforin IIb, purified by nickel nitrilo-triacetic acid (Ni-NTA) resin chromatography, was cleaved by hydroxylamine hydrochloride to release recombinant buforin IIb. Purification of recombinant buforin IIb was achieved by HPLC: about 3.1 mg/l active recombinant buforin IIb with purity >99% was obtained. The recombinant buforin IIb showed antimicrobial activities that were similar to the synthetic one. |
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