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• W1794689920 abstract "Pathology in Parkinson's disease is linked to self-association of α-Synuclein (αS) into pathogenic oligomeric species and highly ordered amyloid fibrils. Developing effective therapeutic strategies against this debilitating disease is critical and βS, a pre-synaptic protein that co-localizes with αS, can act as an inhibitor of αS assembly. Despite the potential importance of βS as an inhibitor of αS, the nature, location and specificity of the molecular interactions between these two proteins is unknown. Here we use NMR paramagnetic relaxation enhancement experiments, to demonstrate that βS interacts directly with αS in a transient dimer complex with high specificity and weak affinity. Inhibition of αS by βS arises from transient αS/βS heterodimer species that exist primarily in head- to- tail configurations while αS aggregation arises from a more heterogeneous and weaker range of transient interactions that include both head-to-head and head-to-tail configurations. Our results highlight that intrinsically disordered proteins can interact directly with one another at low affinity and that the transient interactions that drive inhibition versus aggregation are distinct by virtue of their plasticity and specificity." @default.
• W1794689920 created "2016-06-24" @default.
• W1794689920 creator A5036165542 @default.
• W1794689920 creator A5073961588 @default.
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• W1794689920 date "2015-10-19" @default.
• W1794689920 modified "2023-10-16" @default.
• W1794689920 title "Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein" @default.
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• W1794689920 doi "https://doi.org/10.1038/srep15164" @default.
• W1794689920 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4609965" @default.
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