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.
Highlights
Методом микроэлектрофореза исследовано влияние нативной и амилодной форм лизоцима и сывороточного альбумина на электрокинетическое поведение моно- и мультиламеллярных липосом из цвиттерионного липида фосфатидилхолина и анионного липида кардиолипина
Electrostatics controls a wide variety of processes occurring in cellular membranes, among which are non-specific and specific protein–lipid interactions, protein folding, translocation and orientation in the lipid bilayer [3,4,5], enzyme functioning, ion binding and transport, structural and phase transitions in the lipid phase [1], recognition events [6,7], pharmacological effects [8], etc
Biological membranes consist of hundreds of different molecular species including lipids, proteins and carbohydrates bearing numerous ionized groups which account for the net negative charge of the membrane surface [1]
Summary
In view of a high structural and compositional heterogeneity of biological membranes, a common approach to investigating the above processes is based on the use of the model systems containing isolated proteins in a certain conformational and aggregation state and lipid vesicles (liposomes) whose lipid components and physicochemical parameters can be varied in a wide range. In the present study we used the model protein-lipid systems containing as a protein component lysozyme or serum albumin in the native or fibrillar states and multilamellar lipid vesicles composed of zwitterionic lipid phosphatidylcholine and anionic lipid cardiolipin. Our goal was to obtain a direct evidence for the binding of amyloid fibrils of lysozyme and albumin to lipid vesicles and to compare the effects of the native and fibrillar proteins on the surface charge of lipid bilayer through measuring the electrophoretic mobility of the uni- and multilamellar lipid vesicles
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