Journal
MOLECULES
Volume 22, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/molecules22111963
Keywords
vasoactive intestinal peptide; analogue; recombinant expression; Escherichia coli; antimicrobial activity
Funding
- National Natural Science Foundation of China [31672435, 31702123]
- Shaanxi Provincial Natural Science Foundation [2017JM3025]
- Fundamental Research Funds for the Central Universities [3102015BJ(II)MYZ29, 3102017zy055]
- Graduate Starting Seed Fund of Northwestern Polytechnical University [Z2017237]
- National College Students Innovation Experiment Program [201610699266]
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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 mu M. These findings suggest that VIP analogue 8 is a promising candidate for application as a new and safe antimicrobial agent.
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