Robert W. Newberry

This study shows that modifying the backbone of a minimal NAC-derived peptide with thioamide enhances its ability to modulate α-synuclein aggregation, while N-methylation inhibits it.

The paper uses clickable protein tags to study α-synuclein aggregation in yeast, revealing membrane interactions drive aggregation and identifying key residues that influence this process.

This study uses deep mutational scanning in yeast to show that α-synuclein misfolding and toxicity are concentration-dependent, with mutations altering membrane binding affinity and folding equilibrium.