Exploring two small molecules for the disintegration of alpha-synuclein fibrils UCLA SmallMolecules AlphaSynucleinFibrils Disintegration
Background Parkinson's disease , dementia with Lewy bodies , and multiple system atrophy are neurodegenerative conditions defined by the aberrant accumulation of a protein called alpha-synuclein. This disordered protein makes it difficult to determine its atomic structure in soluble form. Primary and seeded alpha-synuclein aggregation has become a major treatment focus for synucleinopathies.
The team examined ten chemical analogs of CNS-11 to determine if their qualities were similar. Next, the ability of CNS-11g and CNS-11 to dissociate in vitro alpha-synuclein fibrils was assessed. The samples were treated with thioflavin T which was a fluorescent marker for amyloid fibrils, and ThT fluorescence was evaluated. To determine if CNS-11 or CNS-11g affected primary alpha-synuclein aggregation, a ThT aggregation kinetics test was conducted.
There was a slight difference between allowing alpha-synuclein to assemble in the presence of CNS-11 or CNS-11g. When fibril seeds were treated with CNS-11g or CNS-11, the elevation in aggregation time was mitigated, probably due to the preformed fibrils. The fluorescently labeled alpha-synuclein remained soluble at baseline.
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