Design, Recombinant Fusion Expression and Biological Evaluation of Vasoactive Intestinal Peptide Analogue as Novel Antimicrobial Agent.
Molecules
; 22(11)2017 Nov 14.
Article
in En
| MEDLINE
| ID: mdl-29135962
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Recombinant Fusion Proteins
/
Vasoactive Intestinal Peptide
/
Drug Design
/
Anti-Infective Agents
Type of study:
Prognostic_studies
Limits:
Animals
Language:
En
Journal:
Molecules
Journal subject:
BIOLOGIA
Year:
2017
Document type:
Article
Affiliation country:
China