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Amytracker aids in designing small molecules to inhibit aggregation of α-synuclein

Small molecules with the ability to inhibit the nucleation process and stop the aggregation of α-synuclein have immense potential to help people suffering from Parkinson's. Availability of several aSyn protein structures has now opened the possibility to develop structure-based drugs that can specifically bind to and prevent α-synuclein aggregation. In a study, published in Molecular Pharmaceutics, researchers from the Centre for Misfolding Diseases at University of Cambridge aimed to identify such small molecules by using a structure-based drug discovery approach.

First, they performed structure-based in-silico screening of small molecules that can bind to the aSyn and later experimentally verified the obtained best hits. Based on the predicted binding scores they selected 1000 candidates and grouped them in 78 clusters based on similarity. Next, they screened the molecules in an in-vitro chemical kinetics-based assay of α-synuclein aggregation. In their assay, they found 5 compounds that show aggregation inhibitory effect among They most potent candidate was shown to bind to α-synuclein aggregates specifically confirmed by co-staining with Amytracker 630. (Image: Co-staining of the most potent molecule binding to α-synuclein with Amytracker 630. Image from Figure 5D by Chia et al. (2022) Molecular Pharmaceutics, 20(1), 183–193 (CC BY 4.0)).

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