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Antibacterial mechanisms of GN‐2 derived peptides and peptoids against Escherichia coli
Author(s) -
Saporito Paola,
Mojsoska Biljana,
Løbner Olesen Anders,
Jenssen Håvard
Publication year - 2019
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.23275
Subject(s) - biofilm , antimicrobial , chemistry , escherichia coli , antimicrobial peptides , peptide , antibiotics , bacteria , membrane , microbiology and biotechnology , hemolysis , combinatorial chemistry , biochemistry , biology , organic chemistry , genetics , gene , immunology
Escherichia coli is the main etiological agent of urinary trait infections, able to form biofilms in indwelling devices, resulting in chronic infections which are refractory to antibiotics treatment. In this study, we investigated the antimicrobial and anti‐biofilm properties exerted against E. coli ATCC 25922, by a set of peptoids and peptides modeled upon the peptide GN‐2, previously reported as a valid antimicrobial agent. The putative antimicrobials were designed to evaluate the effect of cationicity, hydrophobicity and their partitioning on the overall properties against planktonic cells and biofilms as well as on LPS binding, permeabilization of Gram‐negative bacteria membranes and hemolysis. The data demonstrated that peptides are stronger antimicrobials than the analogue peptoids which in return have superior anti‐biofilm properties. In this study, we present evidence that peptides antimicrobial activity correlates with enhanced LPS binding and hydrophobicity but is not affected by partitioning. The data demonstrated that the enhanced anti‐biofilm properties of the peptoids are associated with decreased hydrophobicity and increased penetration of the inner membrane, compared to that of their peptide counterpart, suggesting that the characteristic flexibility of peptoids or their lack of H‐bonding donors in their backbone, would play a role in their ability to penetrate bacterial membranes.