Hammond, K;
Ryadnov, MG;
Hoogenboom, BW;
(2021)
Atomic force microscopy to elucidate how peptides disrupt membranes.
Biochimica et Biophysica Acta (BBA) - Biomembranes
, 1863
(1)
, Article 183447. 10.1016/j.bbamem.2020.183447.
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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.
Type: | Article |
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Title: | Atomic force microscopy to elucidate how peptides disrupt membranes |
Location: | Netherlands |
Open access status: | An open access version is available from UCL Discovery |
DOI: | 10.1016/j.bbamem.2020.183447 |
Publisher version: | https://doi.org/10.1016/j.bbamem.2020.183447 |
Language: | English |
Additional information: | This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions. |
Keywords: | Antimicrobial peptides, Atomic force microscopy, High resolution imaging, Membrane disruption, Phospholipid membranes, Supported lipid bilayers |
UCL classification: | UCL UCL > Provost and Vice Provost Offices > UCL BEAMS UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Physics and Astronomy |
URI: | https://discovery.ucl.ac.uk/id/eprint/10108816 |
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