<br/>We demonstrate the use of non-resonant angle-resolved second harmonic scattering for detecting the binding of proteins to liposomes in a dilute solution through changes in water orientational correlations. The method can thus be used as high accuracy and high throughput label-free probe of protein-liposome interactions. As an example we investigate the interaction of α-synuclein with 100 nm liposomes in solution. The protein α-synuclein forms amyloids that promote neurodegeneration in Parkinson’s disease. The normal function of α-synuclein includes synaptic vesicle transport and fusion, and the protein binds strongly to negatively charged vesicles in-vitro. Our results support a binding model in which the N-terminus of α-synuclein adopts an α-helical conformation that lies flat on the vesicle surface while the negatively-charged C-terminus remains hydrated in solution.

Membrane-protein-hydration interaction of α-synuclein with anionic vesicles in solution probed via angle-resolved second harmonic scattering

2019 Fall National Meeting

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