Enhancing membrane disruption by targeting and multivalent presentation of antimicrobial peptides

Cristina Chamorro; Marcel A. Boerman; Christopher J. Arnusch; Eefjan Breukink; Roland J. Pieters

doi:https://doi.org/10.1016/j.bbamem.2012.04.004

Enhancing membrane disruption by targeting and multivalent presentation of antimicrobial peptides

Cristina Chamorro, Marcel A. Boerman, Christopher J. Arnusch, Eefjan Breukink, Roland J. Pieters

Zuckerberg Institute for Water Research

Ben-Gurion University of the Negev

Research output: Contribution to journal › Article › peer-review

Abstract

In order to enhance the membrane disruption of antimicrobial peptides both targeting and multivalent presentation approaches were explored. The antimicrobial peptides anoplin and temporin L were conjugated via click chemistry to vancomycin and to di- and tetravalent dendrimers. The vancomycin unit led to enhanced membrane disruption of large unilamellar vesicles (LUVs) displaying the vancomycin target lipid II, but only for temporin L and not for anoplin. The multivalent presentation led to enhanced LUV membrane disruption in the case of anoplin but not for temporin L.

Original language	American English
Pages (from-to)	2171-2174
Number of pages	4
Journal	Biochimica et Biophysica Acta - Biomembranes
Volume	1818
Issue number	9
DOIs	https://doi.org/10.1016/j.bbamem.2012.04.004
State	Published - 1 Sep 2012

Keywords

Anoplin
Antimicrobial peptide
Membrane disruption
Multivalency
Targeting
Temporin L

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Cell Biology

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https://doi.org/10.1016/j.bbamem.2012.04.004

Cite this

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title = "Enhancing membrane disruption by targeting and multivalent presentation of antimicrobial peptides",

abstract = "In order to enhance the membrane disruption of antimicrobial peptides both targeting and multivalent presentation approaches were explored. The antimicrobial peptides anoplin and temporin L were conjugated via click chemistry to vancomycin and to di- and tetravalent dendrimers. The vancomycin unit led to enhanced membrane disruption of large unilamellar vesicles (LUVs) displaying the vancomycin target lipid II, but only for temporin L and not for anoplin. The multivalent presentation led to enhanced LUV membrane disruption in the case of anoplin but not for temporin L.",

keywords = "Anoplin, Antimicrobial peptide, Membrane disruption, Multivalency, Targeting, Temporin L",

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AU - Chamorro, Cristina

AU - Boerman, Marcel A.

AU - Arnusch, Christopher J.

AU - Breukink, Eefjan

AU - Pieters, Roland J.

PY - 2012/9/1

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AB - In order to enhance the membrane disruption of antimicrobial peptides both targeting and multivalent presentation approaches were explored. The antimicrobial peptides anoplin and temporin L were conjugated via click chemistry to vancomycin and to di- and tetravalent dendrimers. The vancomycin unit led to enhanced membrane disruption of large unilamellar vesicles (LUVs) displaying the vancomycin target lipid II, but only for temporin L and not for anoplin. The multivalent presentation led to enhanced LUV membrane disruption in the case of anoplin but not for temporin L.

KW - Anoplin

KW - Antimicrobial peptide

KW - Membrane disruption

KW - Multivalency

KW - Targeting

KW - Temporin L

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Enhancing membrane disruption by targeting and multivalent presentation of antimicrobial peptides

Abstract

Keywords

All Science Journal Classification (ASJC) codes

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