Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: a comparative study of different backbones

Rasmus D Jahnsen; Niels Frimodt-Møller; Henrik Franzyk

doi:10.1021/jm300820a

Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: a comparative study of different backbones

Rasmus D Jahnsen, Niels Frimodt-Møller, Henrik Franzyk

54 Citationer (Scopus)

Abstract

Novel remedies in the battle against multidrug-resistant bacterial strains are urgently needed, and one obvious approach involves antimicrobial peptides and mimics hereof. The impact of α- and β-peptoid as well as β³-amino acid modifications on the activity profile against β-lactamase-producing Escherichia coli was assessed by testing an array comprising different types of cationic peptidomimetics obtained by a general monomer-based solid-phase synthesis protocol. Most of the peptidomimetics possessed high to moderate activity toward multidrug-resistant E. coli as opposed to the corresponding inactive peptides. Nevertheless, differences in hemolytic activities indicate that a careful choice of backbone design constitutes a significant parameter in the search for effective cationic antimicrobial peptidomimetics targeting specific bacteria.

Originalsprog	Engelsk
Tidsskrift	Journal of Medicinal Chemistry
Vol/bind	55
Udgave nummer	16
Sider (fra-til)	7253-61
Antal sider	9
ISSN	0022-2623
DOI	https://doi.org/10.1021/jm300820a
Status	Udgivet - 23 aug. 2012

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10.1021/jm300820a

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AU - Franzyk, Henrik

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AB - Novel remedies in the battle against multidrug-resistant bacterial strains are urgently needed, and one obvious approach involves antimicrobial peptides and mimics hereof. The impact of α- and β-peptoid as well as β3-amino acid modifications on the activity profile against β-lactamase-producing Escherichia coli was assessed by testing an array comprising different types of cationic peptidomimetics obtained by a general monomer-based solid-phase synthesis protocol. Most of the peptidomimetics possessed high to moderate activity toward multidrug-resistant E. coli as opposed to the corresponding inactive peptides. Nevertheless, differences in hemolytic activities indicate that a careful choice of backbone design constitutes a significant parameter in the search for effective cationic antimicrobial peptidomimetics targeting specific bacteria.

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JO - Journal of Medicinal Chemistry

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ER -

Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: a comparative study of different backbones

Abstract

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