Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles

摘要: Amyloid seeds are nanometre-sized protein particles that accelerate amyloid assembly, as well propagate and transmit the conformation associated with a wide range of misfolding diseases. However, seeded growth through templated elongation at fibril ends cannot explain full molecular behaviours observed during cross-seeded formation by heterologous seeds. Here, we demonstrate can via surface catalysis mechanism without propagating specific This type seeding is demonstrated quantitative characterisation assembly reactions involving two non-homologous unrelated proteins: human A{beta}42 peptide yeast prion-forming Sup35NM. Our results suggest experimental approaches to differentiate from non-templated seeding, rationalise cross-seeding phenomenon manifestation aberrant activities presented nanoparticles.