Förster resonance energy transfer evidence for lysozyme oligomerization in lipid environment.
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.
Department of Biological and Medical Physics, V. N. Karazin Kharkov National University, 4 Svobody Sq., Kharkov 61077, Ukraine. valtrusova@yahoo.com
Valeriya M
VM
Trusova
Galyna P
GP
Gorbenko
Pabak
P
Sarkar
Rafal
R
Luchowski
Irina
I
Akopova
Leonid D
LD
Patsenker
Oleksii
O
Klochko
Anatoliy L
AL
Tatarets
Yuliia O
YO
Kudriavtseva
Ewald A
EA
Terpetschnig
Ignacy
I
Gryczynski
Zygmunt
Z
Gryczynski
D031541:Fluorescence Resonance Energy Transfer; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry*; D010713:Phosphatidylcholines / Q000737:chemistry*; D010715:Phosphatidylglycerols / Q000737:chemistry; D058105:Polymerization
D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; D009113:Muramidase