Atomic force microscopy to elucidate how peptides disrupt membranes

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.

Automated summary

Atomic force microscopy is increasingly used to study how peptides disrupt membranes, providing nanometer resolution for dynamic investigations on lipid bilayers. Over the past decade, AFM studies have visualized membrane disruption mechanisms by antimicrobial peptides targeting malignant cells and biofilms. The emergence of high-speed modalities in AFM enables investigations on antimicrobial kinetics and real-time imaging of peptide action on live cells.