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1

Department of Chemical Engineering, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 40227, Taiwan

2

Biotechnology Center, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 40227, Taiwan





*

Author to whom correspondence should be addressed.



Academic Editors: Fernando Albericio and Derek J. McPhee

Abstract Cecropin is a cationic antibacterial peptide composed of 35–39 residues. This peptide has been identified as possessing strong antibacterial activity and low toxicity against eukaryotic cells, and it has been claimed that some types of the cecropin family of peptides are capable of killing cancer cells. In this study, the host effect of cloning antibacterial peptide cecropinB2 was investigated. Three different host expression systems were chosen, i.e., Escherichia coli, Bacillus subtilis and Pichia pastoris. Two gene constructs, cecropinB2 cecB2 and intein-cecropinB2 INT-cecB2, were applied. Signal peptide and propeptide from Armigeres subalbatus were also attached to the gene construct. The results showed that the best host for cloning cecropinB2 was P. pastoris SMD1168 harboring the gene of pGAPzαC-prepro-cecB2 via Western blot confirmation. The cecropinB2 that was purified using immobilized-metal affinity chromatography resin showed strong antibacterial activity against the Gram-negative strains, including the multi-drug-resistant bacteria Acinetobacter baumannii. View Full-Text

Keywords: cecropinB2; antibacterial peptides; multi-drug-resistant; Pichia pastoris; Bacillus subtilis cecropinB2; antibacterial peptides; multi-drug-resistant; Pichia pastoris; Bacillus subtilis





Autor: Wei-Shiang Lai 1, Shu-Chen Kan 1, Chia-Chi Lin 1, Chwen-Jen Shieh 2 and Yung-Chuan Liu 1,*

Fuente: http://mdpi.com/



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