Design, recombinant fusion expression and biological evaluation of vasoactive intestinal peptide analogue as novel antimicrobial agent

Chunlan Xu, Yu Guo, Xiangjin Qiao, Xiaoya Shang, Weining Niu, Mingliang Jin

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

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.

Original languageEnglish
Article number1963
JournalMolecules
Volume22
Issue number11
DOIs
StatePublished - Nov 2017

Keywords

  • Analogue
  • Antimicrobial activity
  • Escherichia coli
  • Recombinant expression
  • Vasoactive intestinal peptide

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