Azad Farzadfard

This study uses systematic K-to-Q mutagenesis to probe the energy landscape of α-Synuclein aggregation, identifying core residue mutations that alter free energy pathways and fibril polymorphism.

This study shows that terminal truncations of α-synuclein significantly alter phase separation, while familial mutations have minimal effects, influencing amyloid fibril formation and condensate behavior.

This study shows that the Bri2 BRICHOS domain inhibits α-synuclein oligomer formation and toxicity by suppressing secondary nucleation and binding oligomers, suggesting its potential as a therapeutic target for Parkinson's disease.