Dev Thacker

This study shows that sequence imperfections in synthetic Aβ42 peptides cause differences in aggregation behavior compared to recombinant Aβ42.

This study shows that structural defects in amyloid-β fibrils are key sites for secondary nucleation, suggesting new strategies for drug design to inhibit amyloid disorders.

This paper investigates how aducanumab binds to Aβ1-42 fibrils, showing it preserves the fibril core structure while altering N-terminal dynamics and reducing secondary nucleation.

This study identifies residues 2-7 of alpha-synuclein as regulators of amyloid formation, showing they slow fibril formation and reduce aggregation in vitro and in vivo without affecting membrane binding.