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Atomic force microscopy to elucidate how peptides disrupt membranes.

Authors
  • Hammond, Katharine1
  • Ryadnov, Maxim G2
  • Hoogenboom, Bart W3
  • 1 National Physical Laboratory, Hampton Road, Teddington TW11 0LW, UK; London Centre for Nanotechnology, University College London, London WC1H 0AH, UK; Department of Physics & Astronomy, University College London, London WC1E 6BT, UK. Electronic address: [email protected]
  • 2 National Physical Laboratory, Hampton Road, Teddington TW11 0LW, UK; Department of Physics, King's College London, Strand Lane, London WC2R 2LS, UK. Electronic address: [email protected]
  • 3 London Centre for Nanotechnology, University College London, London WC1H 0AH, UK; Department of Physics & Astronomy, University College London, London WC1E 6BT, UK. Electronic address: [email protected]
Type
Published Article
Journal
Biochimica et biophysica acta. Biomembranes
Publication Date
Jan 01, 2021
Volume
1863
Issue
1
Pages
183447–183447
Identifiers
DOI: 10.1016/j.bbamem.2020.183447
PMID: 32835656
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Atomic force microscopy is an increasingly attractive tool to study how peptides disrupt membranes. Often performed on reconstituted lipid bilayers, it provides access to time and length scales that allow dynamic investigations with nanometre resolution. Over the last decade, AFM studies have enabled visualisation of membrane disruption mechanisms by antimicrobial or host defence peptides, including peptides that target malignant cells and biofilms. Moreover, the emergence of high-speed modalities of the technique broadens the scope of investigations to antimicrobial kinetics as well as the imaging of peptide action on live cells in real time. This review describes how methodological advances in AFM facilitate new insights into membrane disruption mechanisms. Copyright © 2020 Elsevier B.V. All rights reserved.

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