| Literature DB >> 32835656 |
Katharine Hammond1, Maxim G Ryadnov2, Bart W Hoogenboom3.
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.Keywords: Antimicrobial peptides; Atomic force microscopy; High resolution imaging; Membrane disruption; Phospholipid membranes; Supported lipid bilayers
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Year: 2020 PMID: 32835656 DOI: 10.1016/j.bbamem.2020.183447
Source DB: PubMed Journal: Biochim Biophys Acta Biomembr ISSN: 0005-2736 Impact factor: 3.747