Sheena E. Radford

TL;DR: Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.

TL;DR: This work describes the construction of oligopeptides, rationally designed or based on segments of native proteins, that aggregate in suitable solvents into long, semi-flexible β-sheet tapes and suggests that it should be possible to engineer a wide range of properties in these gels by appropriate choice of the peptide primary structure.

TL;DR: It is shown that nanoparticles (copolymer particles, cerium oxide particles, quantum dots, and carbon nanotubes) enhance the probability of appearance of a critical nucleus for nucleation of protein fibrils from human β2-microglobulin, and the shortened lag phase suggest a mechanism involving surface-assisted nucleation that may increase the risk for toxic cluster and amyloid formation.

TL;DR: Analysis of the folding of hen lysozyme shows that the protein does not become organized in a single cooperative event but that different parts of the structure become stabilized with very different kinetics.

TL;DR: The first near-atomic-resolution structures of amyloid fibrils formed in vitro, seeded from plaque material and analysed directly ex vivo are now available and reveal cross-β structures that are far more intricate than anticipated.