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Open AccessArticle

Design, Recombinant Fusion Expression and Biological Evaluation of Vasoactive Intestinal Peptide Analogue as Novel Antimicrobial Agent

The Key Laboratory for Space Bioscience and Biotechnology, School of Life Sciences, Northwestern Polytechnical University, Xi’an 710072, China
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Molecules 2017, 22(11), 1963; https://doi.org/10.3390/molecules22111963
Received: 12 October 2017 / Accepted: 8 November 2017 / Published: 14 November 2017
(This article belongs to the Special Issue Antimicrobial Peptides and Peptidomimetics)
Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity. Modified vasoactive intestinal peptide (VIP) (VIP analogue 8 with amino acid sequence “FTANYTRLRRQLAVRRYLAAILGRR”) without haemolytic activity and cytotoxicity displayed enhanced antimicrobial activities against Staphylococcus aureus (S. aureus) ATCC 25923 and Escherichia coli (E. coli) ATCC 25922 than parent VIP even in the presence of 180 mM NaCl or 50 mM MgCl2, or in the range of pH 4–10. VIP analogue 8 was expressed as fusion protein thioredoxin (Trx)-VIP8 in E. coli BL21(DE) at a yield of 45.67 mg/L. The minimum inhibitory concentration (MIC) of the recombinant VIP analogue 8 against S. aureus ATCC 25923 and E. coli ATCC 25922 were 2 μM. These findings suggest that VIP analogue 8 is a promising candidate for application as a new and safe antimicrobial agent. View Full-Text
Keywords: vasoactive intestinal peptide; analogue; recombinant expression; Escherichia coli; antimicrobial activity vasoactive intestinal peptide; analogue; recombinant expression; Escherichia coli; antimicrobial activity
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MDPI and ACS Style

Xu, C.; Guo, Y.; Qiao, X.; Shang, X.; Niu, W.; Jin, M. Design, Recombinant Fusion Expression and Biological Evaluation of Vasoactive Intestinal Peptide Analogue as Novel Antimicrobial Agent. Molecules 2017, 22, 1963.

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