Abstract
Many lipids and membrane proteins spontaneously co-cluster and oligomerize in cellular plasma membranes into larger (functional) units, whose detailed characterization requires high spatial resolution. In this contribution, we introduce a powerful spectroscopy/microscopy approach called MC-FRET developed for the analysis of in-membrane nanoscopic aggregation of lipids and proteins in biological membranes.
The approach is based on Förster resonance energy transfer (FRET) occurring in membranes between fluorescently labelled lipids/proteins and subsequent analysis of data by Monte-Carlo simulations. The following applications of MC-FRET are presented here: (1) determination of lipid nanodomain sizes and their surface density; (2) characterization of inter-leaflet organization of lipid nanodomains and (3) the analysis of dimerization of in-membrane proteins.