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

Loading next page...
 
/lp/wiley/molecular-design-of-antimicrobial-peptides-based-on-hemagglutinin-T0VrxgFuQh
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

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off