Abstract
Understanding the mechanisms by which membrane-active molecules exert their action would benefit greatly from direct observation of the dynamics of the interactions and quantitative insights into the degree of physical restructuring and reordering. We previously developed a correlated total-internal reflectance fluorescence-atomic force microscopy (TIRF-AFM) platform that enabled direct determination of local order within the membrane [Oreopoulos and Yip, 2009] We report here the results of a study into the interactions of a series of variants of alpha-synuclein, a presynaptic protein that plays a key role in the pathogenesis of Parkinson's disease, with model membranes. These studies illustrate the role of membrane composition and fluidity on alpha-synuclein self-association and provide direct evidence of membrane reordering. This studies portend the application of related correlated approaches, including coupled ATR-FTIR-AFM for examining conformational changes upon membrane-induced aggregation.
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