High-Level Production of a Novel Antimicrobial Peptide Perinerin in <Emphasis Type="Italic">Escherichia coli</Emphasis> by Fusion Expression |
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Authors: | Qing-Feng Zhou Xue-Gang Luo Liang Ye Tao Xi |
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Institution: | (1) Department of Marine Biochemistry Engineer, School of Life Science and Technology China Pharmaceutical University, Nanjing, 210009, People’s Republic of China |
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Abstract: | Perinerin is a small antimicrobial peptide (AMP) isolated from an Asian marine clamworm, Perinereis aibuhitensis Grube. It shows marked activity in vitro against both Gram-negative and Gram-positive bacteria. To obtain it in large amounts, the coding sequence of perinerin was cloned into pET32a(+) vector and expression as a Trx fusion protein in Escherichia coli. The soluble fusion protein collected from the supernatant of the cell lyste was separated by Ni2+-chelating chromatography. The purified protein was then cleaved by Factor Xa protease to release mature perinerin. Final
purification was achieved by ion-exchange chromatography. Recombinant perinerin exhibited a similar antimicrobial activity
to the native perinerin. These works might provide a significant foundation for the following research on the action of mechanism
of marine AMPs. |
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