Characterization of a proteolytically stable multifunctional host defense peptidomimetic

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Characterization of a proteolytically stable multifunctional host defense peptidomimetic. / Jahnsen, Rasmus D; Haney, Evan F; Franzyk, Henrik; Hancock, Robert E W.

In: Chemistry & Biology, Vol. 20, No. 10, 10.10.2013, p. 1286-1295.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Jahnsen, RD, Haney, EF, Franzyk, H & Hancock, REW 2013, 'Characterization of a proteolytically stable multifunctional host defense peptidomimetic' Chemistry & Biology, vol. 20, no. 10, pp. 1286-1295. https://doi.org/10.1016/j.chembiol.2013.09.007

APA

Jahnsen, R. D., Haney, E. F., Franzyk, H., & Hancock, R. E. W. (2013). Characterization of a proteolytically stable multifunctional host defense peptidomimetic. Chemistry & Biology, 20(10), 1286-1295. https://doi.org/10.1016/j.chembiol.2013.09.007

Vancouver

Jahnsen RD, Haney EF, Franzyk H, Hancock REW. Characterization of a proteolytically stable multifunctional host defense peptidomimetic. Chemistry & Biology. 2013 Oct 10;20(10):1286-1295. https://doi.org/10.1016/j.chembiol.2013.09.007

Author

Jahnsen, Rasmus D ; Haney, Evan F ; Franzyk, Henrik ; Hancock, Robert E W. / Characterization of a proteolytically stable multifunctional host defense peptidomimetic. In: Chemistry & Biology. 2013 ; Vol. 20, No. 10. pp. 1286-1295.

Bibtex

@article{358c34444684491bba0499fe0b059bb8,
title = "Characterization of a proteolytically stable multifunctional host defense peptidomimetic",
abstract = "The in vitro activity of a host defense peptidomimetic (HDM-4) was investigated. The compound exhibited an antimicrobial activity profile against a range of Gram-negative bacteria. HDM-4 permeabilized the outer membrane and partly depolarized the inner membrane at its minimal inhibitory concentration (MIC). Moreover, it was demonstrated that HDM-4 was distributed widely in the bacterial cell at lethal concentrations, and that it could bind to DNA. It was confirmed that the multimodal action of HDM-4 resulted in it being less likely to lead to resistance development as compared to single-target antibiotics. HDM-4 exhibited multispecies anti-biofilm activity at sub-MIC levels. Furthermore, HDM-4 modulated the immune response by inducing the release of the chemoattractants interleukin-8 (IL-8), monocyte chemotactic protein-1 (MCP-1), and MCP-3 from human peripheral blood mononuclear cells. In addition, the compound suppressed lipopolysaccharide-mediated inflammation by reducing the release of the pro-inflammatory cytokines IL-6 and tumor necrosis factor-α.",
author = "Jahnsen, {Rasmus D} and Haney, {Evan F} and Henrik Franzyk and Hancock, {Robert E W}",
note = "Copyright {\circledC} 2013 Elsevier Ltd. All rights reserved.",
year = "2013",
month = "10",
day = "10",
doi = "10.1016/j.chembiol.2013.09.007",
language = "English",
volume = "20",
pages = "1286--1295",
journal = "Chemistry and Biology",
issn = "2451-9448",
publisher = "Elsevier",
number = "10",

}

RIS

TY - JOUR

T1 - Characterization of a proteolytically stable multifunctional host defense peptidomimetic

AU - Jahnsen, Rasmus D

AU - Haney, Evan F

AU - Franzyk, Henrik

AU - Hancock, Robert E W

N1 - Copyright © 2013 Elsevier Ltd. All rights reserved.

PY - 2013/10/10

Y1 - 2013/10/10

N2 - The in vitro activity of a host defense peptidomimetic (HDM-4) was investigated. The compound exhibited an antimicrobial activity profile against a range of Gram-negative bacteria. HDM-4 permeabilized the outer membrane and partly depolarized the inner membrane at its minimal inhibitory concentration (MIC). Moreover, it was demonstrated that HDM-4 was distributed widely in the bacterial cell at lethal concentrations, and that it could bind to DNA. It was confirmed that the multimodal action of HDM-4 resulted in it being less likely to lead to resistance development as compared to single-target antibiotics. HDM-4 exhibited multispecies anti-biofilm activity at sub-MIC levels. Furthermore, HDM-4 modulated the immune response by inducing the release of the chemoattractants interleukin-8 (IL-8), monocyte chemotactic protein-1 (MCP-1), and MCP-3 from human peripheral blood mononuclear cells. In addition, the compound suppressed lipopolysaccharide-mediated inflammation by reducing the release of the pro-inflammatory cytokines IL-6 and tumor necrosis factor-α.

AB - The in vitro activity of a host defense peptidomimetic (HDM-4) was investigated. The compound exhibited an antimicrobial activity profile against a range of Gram-negative bacteria. HDM-4 permeabilized the outer membrane and partly depolarized the inner membrane at its minimal inhibitory concentration (MIC). Moreover, it was demonstrated that HDM-4 was distributed widely in the bacterial cell at lethal concentrations, and that it could bind to DNA. It was confirmed that the multimodal action of HDM-4 resulted in it being less likely to lead to resistance development as compared to single-target antibiotics. HDM-4 exhibited multispecies anti-biofilm activity at sub-MIC levels. Furthermore, HDM-4 modulated the immune response by inducing the release of the chemoattractants interleukin-8 (IL-8), monocyte chemotactic protein-1 (MCP-1), and MCP-3 from human peripheral blood mononuclear cells. In addition, the compound suppressed lipopolysaccharide-mediated inflammation by reducing the release of the pro-inflammatory cytokines IL-6 and tumor necrosis factor-α.

U2 - 10.1016/j.chembiol.2013.09.007

DO - 10.1016/j.chembiol.2013.09.007

M3 - Journal article

VL - 20

SP - 1286

EP - 1295

JO - Chemistry and Biology

JF - Chemistry and Biology

SN - 2451-9448

IS - 10

ER -

ID: 56064391