EFFECT OF AMYLOID FIBRILS ON ELECTROKINETIC PROPERTIES OF LIPID VESICLES

Abstract

The influence of the lysozyme and serum albumin in their native and amyloid forms on the electrokinetic behavior of the negatively charged uni- and multilamellar liposomes from the zwitterionic lipid phosphatidylcholine and anionic lipid cardiolipin has been investigated using the microelectrophoresis technique. The zeta - potential, the surface electrostatic potential and surface charge density of the lipid vesicles have been determined upon varying the lipid-to-protein molar ratio. The complex dependencies of the electrophoretic mobility on the protein concentration and reversal of the surface charge observed for the multilamellar vesicles have been explained by the multilayer protein adsorption on the liposomal surface. It has been found that the native and fibrillar proteins differ in their ability to modify the charge state of the model membranes.

Keywords

• electrophoretic mobility
• lipid vesicles
• lysozyme
• serum albumin
• amyloid fibrils