Abstract
The intrinsically disordered protein α-synuclein causes Parkinson's disease by forming toxic oligomeric aggregates inside neurons. Single-molecule FRET experiments revealed conformational changes of noncanonical DNA structures, such as i-motifs and hairpins, in the presence of α-synuclein. Volumetric analyses revealed differences in binding mode, which is also affected by cellular osmolytes.
Highlights
The intrinsically disordered protein a-synuclein causes Parkinson’s disease by forming toxic oligomeric aggregates inside neurons
Parkinson’s disease (PD) arises because of abnormal aggregation of a-Syn, and these aggregates are dominantly found in Lewy bodies as the hallmark of PD.[1,2,3]
The toxic aggregated form of a-Syn detected in PD affected brain as well as other amyloidogenic proteins, such as the prion protein (PrP), have a high propensity to interact with DNA.[3,8,9,10,11,12]
Summary
The intrinsically disordered protein a-synuclein causes Parkinson’s disease by forming toxic oligomeric aggregates inside neurons.
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