ESR imaging of myelin basic protein induced vesicle aggregation.
Using a modulated magnetic field gradient technique, the conventional ESR spectrum of well-defined spatial sections and the one-dimensional-ESR image of the nitroxide centre line of spin-labeled stearic acid in phospholipid vesicles were recorded with a spatial resolution of 4.10(-5) m after pelleting the vesicles inside 1 mm (i.d.) sample capillaries in a slow centrifuge (2500 X g). The sedimentation characteristics of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol vesicles were quantitatively compared with particular reference to vesicle aggregation induced by myelin basic protein. Protein-induced changes in the effective molecular mass were determined from ESR images of sedimentation profiles. The present data lend further support to the notion that the primary target of myelin basic protein-lipid interaction is the acidic lipid pool of myelin.
D004134:Dimyristoylphosphatidylcholine; D004578:Electron Spin Resonance Spectroscopy / Q000295:instrumentation / Q000379:methods; D008081:Liposomes; D008954:Models, Biological; D008968:Molecular Conformation; D004676:Myelin Basic Protein; D010715:Phosphatidylglycerols
D008081:Liposomes; D004676:Myelin Basic Protein; D010715:Phosphatidylglycerols; C002773:dimyristoylphosphatidylglycerol; D004134:Dimyristoylphosphatidylcholine