2013
Volume 13, Number 3, pp. 77–84
Interaction of lysozyme amyloid fibrils with Langmuir monolayers
A. Yudintseva,1 V. Trusova,1 G. Gorbenko,1 R. Volinsky,2 R. Sood2 and P. Kinnunen2
1 Department of Nuclear and Medical Physics, V.N. Karazin Kharkov National University, 4 Svobody Sq., 61022 Kharkov, Ukraine
2 Department of Biomedical Engineering and Computational Science, School of Science and Technology, Aalto University, 00076 Espoo, Finland
The capability of amyloid lysozyme fibrils to insert into phospholipid monolayers composed of dimyristoylphosphatidylcholine (DMPC) and its mixtures with dimyristoylphosphatidylglycerol (DMPG) or dimyristoylphosphatidylserine (DMPS) in different molar ratios was studied using the Langmuir monolayer technique. Fibrillar lysozyme was found to possess a greater ability to penetrate the lipid monolayer compared to the native protein. Electrostatic interactions between cationic groups of the protein and negatively charged head groups of the phospholipids were shown to play a significant rôle in the insertion of lysozyme fibrils and monomers into the model membranes. Evaluation of the limiting surface pressure suggests that both lysozyme monomers and fibrils are able to insert into biological membranes.