title: Probing protein-lipid interactions by FRET between membrane fluorophores.
abstract: Förster resonance energy transfer (FRET) is a powerful fluorescence technique that has found numerous applications in medicine and biology. One area where FRET proved to be especially informative involves the intermolecular interactions in biological membranes. The present study was focused on developing and verifying a Monte-Carlo approach to analyzing the results of FRET between the membrane-bound fluorophores. This approach was employed to quantify FRET from benzanthrone dye ABM to squaraine dye SQ-1 in the model protein-lipid system containing a polycationic globular protein lysozyme and negatively charged lipid vesicles composed of phosphatidylcholine and phosphatidylglycerol. It was found that acceptor redistribution between the lipid bilayer and protein binding sites resulted in the decrease of FRET efficiency. Quantification of this effect in terms of the proposed methodology yielded both structural and binding parameters of lysozyme-lipid complexes.
authors.affiliation: Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University, 4 Svobody Sq., Kharkiv 61022, Ukraine. Address to whom any correspondence should be addressed: Valeriya M. Trusova, 19-32 Geroyev Truda Str., Kharkiv 61144, Ukraine.
authors.forename: Valeriya M
authors.initials: VM
authors.lastname: Trusova
authors.forename: Galyna P
authors.initials: GP
authors.lastname: Gorbenko
authors.forename: Todor
authors.initials: T
authors.lastname: Deligeorgiev
authors.forename: Nikolai
authors.initials: N
authors.lastname: Gadjev
mesh_terms: D002462:Cell Membrane; D031541:Fluorescence Resonance Energy Transfer; D005456:Fluorescent Dyes; D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; D011485:Protein Binding
chemical_list: D005456:Fluorescent Dyes; D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols