Molecular design of antimicrobial peptides based on hemagglutinin fusion domain to combat antibiotic resistance in bacterial infection

Molecular design of antimicrobial peptides based on hemagglutinin fusion domain to combat... Antimicrobial peptides are derived from the viral fusion domain of influenza virus hemagglutinin based on rational analysis of the intermolecular interaction between peptides and bacterial outer membrane. It is revealed that the isolated viral fusion domain is a negatively charged peptide HAfp1‐23 that cannot effectively interact with the anionic membrane. Conversion of the native HAfp1‐23 to a positively charged peptide HAfp1‐23_KK by E11K/D19K mutation can promote the peptide‐membrane interaction substantially; this confers to the peptide a moderate antibacterial potency against antibiotic‐resistant bacterial strains. Cyclization of the linear peptide HAfp1‐23_KK results in a cyclic peptide cHAfp1‐23_KK, which can largely minimize entropy penalty upon the peptide‐membrane binding by pre‐stabilizing peptide hairpin configuration in solvent, where the linear peptide would incur in a considerable conformational change/folding from intrinsic disorder (in water) to the structured hairpin conformation (in lipid). As might be expected, the cyclization considerably improves peptide antibacterial activity with minimum inhibitory concentration of 67 and 34 μg/mL against multidrug‐resistant Pseudomonas aeruginosa and methicillin‐resistant Staphylococcus aureus, respectively. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Peptide Science Wiley

Molecular design of antimicrobial peptides based on hemagglutinin fusion domain to combat antibiotic resistance in bacterial infection

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
Copyright © 2018 European Peptide Society and John Wiley & Sons, Ltd.
ISSN
1075-2617
eISSN
1099-1387
D.O.I.
10.1002/psc.3068
Publisher site
See Article on Publisher Site

Abstract

Antimicrobial peptides are derived from the viral fusion domain of influenza virus hemagglutinin based on rational analysis of the intermolecular interaction between peptides and bacterial outer membrane. It is revealed that the isolated viral fusion domain is a negatively charged peptide HAfp1‐23 that cannot effectively interact with the anionic membrane. Conversion of the native HAfp1‐23 to a positively charged peptide HAfp1‐23_KK by E11K/D19K mutation can promote the peptide‐membrane interaction substantially; this confers to the peptide a moderate antibacterial potency against antibiotic‐resistant bacterial strains. Cyclization of the linear peptide HAfp1‐23_KK results in a cyclic peptide cHAfp1‐23_KK, which can largely minimize entropy penalty upon the peptide‐membrane binding by pre‐stabilizing peptide hairpin configuration in solvent, where the linear peptide would incur in a considerable conformational change/folding from intrinsic disorder (in water) to the structured hairpin conformation (in lipid). As might be expected, the cyclization considerably improves peptide antibacterial activity with minimum inhibitory concentration of 67 and 34 μg/mL against multidrug‐resistant Pseudomonas aeruginosa and methicillin‐resistant Staphylococcus aureus, respectively.

Journal

Journal of Peptide ScienceWiley

Published: Jan 1, 2018

Keywords: ; ; ; ; ;

References

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