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

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Standard

Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli : a comparative study of different backbones. / Jahnsen, Rasmus D; Frimodt-Møller, Niels; Franzyk, Henrik.

In: Journal of Medicinal Chemistry, Vol. 55, No. 16, 2012, p. 7253-61.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Jahnsen, RD, Frimodt-Møller, N & Franzyk, H 2012, 'Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: a comparative study of different backbones' Journal of Medicinal Chemistry, vol. 55, no. 16, pp. 7253-61. https://doi.org/10.1021/jm300820a

APA

Jahnsen, R. D., Frimodt-Møller, N., & Franzyk, H. (2012). Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: a comparative study of different backbones. Journal of Medicinal Chemistry, 55(16), 7253-61. https://doi.org/10.1021/jm300820a

Vancouver

Jahnsen RD, Frimodt-Møller N, Franzyk H. Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: a comparative study of different backbones. Journal of Medicinal Chemistry. 2012;55(16):7253-61. https://doi.org/10.1021/jm300820a

Author

Jahnsen, Rasmus D ; Frimodt-Møller, Niels ; Franzyk, Henrik. / Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli : a comparative study of different backbones. In: Journal of Medicinal Chemistry. 2012 ; Vol. 55, No. 16. pp. 7253-61.

Bibtex

@article{dd12bbb594cb4d24803c35e90fd4e0be,
title = "Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli: a comparative study of different backbones",
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 a- and {\ss}-peptoid as well as {\ss}(3)-amino acid modifications on the activity profile against {\ss}-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.",
author = "Jahnsen, {Rasmus D} and Niels Frimodt-M{\o}ller and Henrik Franzyk",
year = "2012",
doi = "10.1021/jm300820a",
language = "English",
volume = "55",
pages = "7253--61",
journal = "Journal of Medicinal Chemistry",
issn = "0022-2623",
publisher = "American Chemical Society",
number = "16",

}

RIS

TY - JOUR

T1 - Antimicrobial activity of peptidomimetics against multidrug-resistant Escherichia coli

T2 - a comparative study of different backbones

AU - Jahnsen, Rasmus D

AU - Frimodt-Møller, Niels

AU - Franzyk, Henrik

PY - 2012

Y1 - 2012

N2 - 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 a- and ß-peptoid as well as ß(3)-amino acid modifications on the activity profile against ß-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.

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 a- and ß-peptoid as well as ß(3)-amino acid modifications on the activity profile against ß-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.

U2 - 10.1021/jm300820a

DO - 10.1021/jm300820a

M3 - Journal article

VL - 55

SP - 7253

EP - 7261

JO - Journal of Medicinal Chemistry

JF - Journal of Medicinal Chemistry

SN - 0022-2623

IS - 16

ER -

ID: 41915115