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1000 Titel
  • Evidence for a Novel Mechanism of Antimicrobial Action of a Cyclic R-,W-Rich HexapeptideEvidence for a Novel Mechanism of Antimicrobial Action of a Cyclic R-,W-Rich Hexapeptide
1000 Autor/in
  1. Scheinpflug, Kathi |
  2. Krylova, Oxana |
  3. Nikolenko, Heike |
  4. Thurm, Charley |
  5. Dathe, Margitta |
1000 Erscheinungsjahr 2015
1000 LeibnizOpen
1000 Art der Datei
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2015-04-15
1000 Erschienen in
1000 Quellenangabe
  • 10(4):e0125056
1000 FRL-Sammlung
1000 Copyrightjahr
  • 2015
1000 Lizenz
1000 Verlagsversion
  • http://dx.doi.org/10.1371/journal.pone.0125056 |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • The development of antimicrobial peptides as new class of antibiotic agents requires structural characterisation and understanding of their diverse mechanisms of action. As the cyclic hexapeptide cWFW (cyclo(RRRWFW)) does not exert its rapid cell killing activity by membrane permeabilisation, in this study we investigated alternative mechanisms of action, such as peptide translocation into the cytoplasm and peptide interaction with components of the phospholipid matrix of the bacterial membrane. Using fluorescence microscopy and an HPLC-based strategy to analyse peptide uptake into the cells we could confirm the cytoplasmic membrane as the major peptide target. However, unexpectedly we observed accumulation of cWFW at distinct sites of the membrane. Further characterisation of peptide-membrane interaction involved live cell imaging to visualise the distribution of the lipid cardiolipin (CL) and isothermal titration calorimetry to determine the binding affinity to model membranes with different bacterial lipid compositions. Our results demonstrate a distribution of the cyclic peptide similar to that of cardiolipin within the membrane and highly preferred affinity of cWFW for CL-rich phosphatidylethanolamine (POPE) matrices. These observations point to a novel mechanism of antimicrobial killing for the cyclic hexapeptide cWFW which is neither based on membrane permeabilisation nor translocation into the cytoplasm but rather on preferred partitioning into particular lipid domains. As the phospholipids POPE/CL play a key role in the dynamic organisation of bacterial membranes we discuss the consequences of this peptide-lipid-interaction and outline the impact on antimicrobial peptide research.
1000 Sacherschließung
lokal Vesicles
lokal Bacillus subtilis
lokal Lipids
lokal Pospholipids
lokal Peptide synthesis
lokal Cytoplasm
lokal Fluorescence microscopy
lokal High performance liquid chromatography
1000 Fachgruppe
  1. Biologie |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/IFNjaGVpbnBmbHVnLCBLYXRoaQ==|https://frl.publisso.de/adhoc/creator/IEtyeWxvdmEsIE94YW5h|https://frl.publisso.de/adhoc/creator/IE5pa29sZW5rbywgSGVpa2U=|https://frl.publisso.de/adhoc/creator/IFRodXJtLCBDaGFybGV5|https://frl.publisso.de/adhoc/creator/IERhdGhlLCBNYXJnaXR0YQ==
1000 Dateien
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1000 Erstellt am 2017-05-26T13:12:50.165+0200
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1000 Zuletzt bearbeitet Wed Aug 01 12:26:54 CEST 2018
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1000 Vgl. frl:6402614
1000 Oai Id
  1. oai:frl.publisso.de:frl:6402614 |
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