Danny D. Sahtoe

Mar 18, 2024 | nature.com | Danny D. Sahtoe |Ewa Andrzejewska |Hannah Han |Matthias Schneider |Georg Meisl |Hannah Nguyen | +2 more

AbstractSegments of proteins with high β-strand propensity can self-associate to form amyloid fibrils implicated in many diseases. We describe a general approach to bind such segments in β-strand and β-hairpin conformations using de novo designed scaffolds that contain deep peptide-binding clefts. The designs bind their cognate peptides in vitro with nanomolar affinities.