Atomic force microscopy to elucidate how peptides disrupt membranes

Biochim Biophys Acta Biomembr. 2021 Jan 1;1863(1):183447. doi: 10.1016/j.bbamem.2020.183447. Epub 2020 Aug 21.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biofilms / drug effects*
  • Cell Membrane* / chemistry
  • Cell Membrane* / metabolism
  • Cell Membrane* / ultrastructure
  • Humans
  • Microscopy, Atomic Force*
  • Neoplasms* / chemistry
  • Neoplasms* / metabolism
  • Neoplasms* / ultrastructure
  • Pore Forming Cytotoxic Proteins* / chemistry
  • Pore Forming Cytotoxic Proteins* / pharmacology

Substances

  • Pore Forming Cytotoxic Proteins