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.
Highlights
As is known to all, a series of disadvantages brought by the application of classical antibiotics makes it urgent to develop promising and alternative antimicrobial strategies
We aimed to design and generate a novel peptide (VIP analogue) with an enhanced antimicrobial potency, low or no-haemolytic activity, and high stability by amino acid substitution based on their physicochemical property and usual antimicrobial mechanism, and establish an effective and low-cost production method by fusion expression of vasoactive intestinal peptide (VIP) analogue with Trx in E. coli
The structure and molecular weights of these peptides were verified by electrospray ionization mass spectrometry (ESI-MS)
Summary
As is known to all, a series of disadvantages brought by the application of classical antibiotics makes it urgent to develop promising and alternative antimicrobial strategies. Antimicrobial peptides represent an emerging category of therapeutic agents with remarkable structural and functional diversity [2]. Many human oral antimicrobial peptides are responsible for playing important roles including maintenance, repairing of oral tissues and defence against oral microbes [3,4]. The role of cationic host-defence peptides in modulating the innate immune response and boosting infection-resolving immunity while dampening harmful pro-inflammatory (septic) responses gives these peptides the potential to become an entirely new therapeutic approach against bacterial infections [5]. Vasoactive intestinal peptide (VIP) is an important signal molecule of the neuroendocrine-immune network [6,7] and plays key roles in a broad spectrum of biological functions including antimicrobial, anti-inflammatory and immune-modulatory activity
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