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Biophys."],"published-print":{"date-parts":[[2017]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Amyloid formation of the synaptic brain protein<jats:italic>\u03b1<\/jats:italic>-synuclein (<jats:italic>\u03b1<\/jats:italic>S) is related to degeneration of dopaminergic neurons in Parkinson's disease patients.<jats:italic>\u03b1<\/jats:italic>S is thought to function in vesicle transport and fusion and it binds strongly to negatively charged vesicles<jats:italic>in vitro<\/jats:italic>. Here we combined circular dichroism, fluorescence and imaging methods<jats:italic>in vitro<\/jats:italic>to characterize the interaction of<jats:italic>\u03b1<\/jats:italic>S with negatively charged vesicles of DOPS (1,2-dioleoyl-<jats:italic>sn-<\/jats:italic>glycero-3-phospho-L-serine, sodium salt) and DOPG (1,2-dioleoyl-<jats:italic>sn-<\/jats:italic>glycero-3-phospho-(1\u2032-<jats:italic>rac<\/jats:italic>-glycerol), sodium salt) and the consequences of such interactions on<jats:italic>\u03b1<\/jats:italic>S amyloid formation. We found that lipid head-group chemistry modulates<jats:italic>\u03b1<\/jats:italic>S interactions and also affects amyloid fiber formation. During the course of the experiments, we made the unexpected discovery that pre-formed<jats:italic>\u03b1<\/jats:italic>S oligomers, typically present in a small amount in the<jats:italic>\u03b1<\/jats:italic>S starting material, acted as templates for linear growth of anomalous amyloid fibers in the presence of vesicles. At the same time, the remaining<jats:italic>\u03b1<\/jats:italic>S monomers were restricted from vesicle-mediated nucleation of amyloid fibers. Although not a dominant process in bulk experiments, this hidden<jats:italic>\u03b1<\/jats:italic>S aggregation pathway may be of importance<jats:italic>in vivo<\/jats:italic>.<\/jats:p>","DOI":"10.1017\/s0033583517000026","type":"journal-article","created":{"date-parts":[[2017,2,10]],"date-time":"2017-02-10T10:58:05Z","timestamp":1486724285000},"source":"Crossref","is-referenced-by-count":27,"title":["Unraveling amyloid formation paths of Parkinson's disease protein \u03b1-synuclein triggered by anionic 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