Designing a Useful Lipid Raft Model Membrane for Electrochemical and Surface Analytical Studies.
Michalina ZaborowskaDamian DziubakDorota MatyszewskaSławomir SękRenata BilewiczPublished in: Molecules (Basel, Switzerland) (2021)
A model biomimetic system for the study of protein reconstitution or drug interactions should include lipid rafts in the mixed lipid monolayer, since they are usually the domains embedding membrane proteins and peptides. Four model lipid films composed of three components: 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), cholesterol (Chol) and sphingomyelin (SM) mixed in different molar ratios were proposed and investigated using surface pressure measurements and thermodynamic analysis of the monolayers at the air-water interface and imaged by Brewster angle microscopy. The ternary monolayers were transferred from the air-water onto the gold electrodes to form bilayer films and were studied for the first time by electrochemical methods: alternative current voltammetry and electrochemical impedance spectroscopy and imaged by atomic force microscopy. In excess of DOPC, the ternary systems remained too liquid for the raft region to be stable, while in the excess of cholesterol the layers were too solid. The layers with SM in excess lead to the formation of Chol:SM complexes but the amount of the fluid matrix was very low. The equimolar content of the three components lead to the formation of a stable and well-organized assembly with well-developed raft microdomains of larger thickness, surrounded by the more fluid part of the bilayer. The latter is proposed as a convenient raft model membrane for further physicochemical studies of interactions with drugs or pollutants or incorporation of membrane proteins.
Keyphrases
- atomic force microscopy
- ionic liquid
- high resolution
- gold nanoparticles
- single molecule
- fatty acid
- room temperature
- optical coherence tomography
- magnetic resonance imaging
- risk assessment
- reduced graphene oxide
- computed tomography
- heavy metals
- low density lipoprotein
- mass spectrometry
- solid state
- simultaneous determination