Förster Resonance Energy Transfer Evidence for Lysozyme Oligomerization in Lipid Environment

Overview

Journal J Phys Chem B

Publisher American Chemical Society

Specialty Chemistry

Date 2010 Dec 4

PMID 21126034

Citations 1

Authors

Valeriya M Trusova

Galyna P Gorbenko

Pabak Sarkar

Rafal Luchowski

Irina Akopova

Leonid D Patsenker

Oleksii Klochko

Anatoliy L Tatarets

Yuliia O Kudriavtseva

Ewald A Terpetschnig

Ignacy Gryczynski

Zygmunt Gryczynski

Affiliations

Soon will be listed here.

Abstract

Intermolecular time-resolved and single-molecule Förster resonance energy transfer (FRET) have been applied to detect quantitatively the aggregation of polycationic protein lysozyme (Lz) in the presence of lipid vesicles composed of phosphatidylcholine (PC) and its mixture with 5, 10, 20, or 40 mol % of phosphatidylglycerol (PG) (PG5, PG10, PG20, or PG40, respectively). Upon binding to PC, PG5, or PG10 model membranes, Lz was found to retain its native monomeric conformation, while increasing content of anionic lipid up to 20 or 40 mol % resulted in the formation of Lz aggregates. The structural parameters of protein self-association (the degree of oligomerization, the distance between the monomers in protein assembly, and the fraction of donors present in oligomers) have been derived. The crucial role of the factors such as lateral density of the adsorbed protein and electrostatic and hydrophobic Lz-lipid interactions in controlling the protein self-association behavior has been proposed.

Citing Articles

Modulation of physiological and pathological activities of lysozyme by biological membranes.

Trusova V Cell Mol Biol Lett. 2012; 17(3):349-75.

PMID: 22544762 PMC: 6275811. DOI: 10.2478/s11658-012-0015-6.

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