Celia Cabaleiro-Lago

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: It is argued that in a biological fluid, proteins associate with nanoparticles, and it is the amount and presentation of the proteins on the surface rather than the particles themselves that are the cause of numerous biological responses.

TL;DR: Copolymeric NiPAM:BAM nanoparticles of varying hydrophobicity were found to retard fibrillation of the Alzheimer's disease-associated amyloid beta protein (Abeta), and numerical analysis of the kinetic data for fibrills suggests that binding of monomeric Abeta and prefibrillar oligomers to the nanoparticles prevents fibrilation.

TL;DR: The fibrillation kinetics of the amyloid β peptide is analyzed in presence of cationic polystyrene nanoparticles of different size and the results highlight the importance of the ratio between the peptide and particle concentration.

TL;DR: For mutants of single-chain monellin differing in intrinsic stability toward denaturation, it is found that amyloid fibril formation is accelerated by nanoparticles, and for mutants with a low intrinsic stability and high intrinsic aggregation rate, the opposite is found—a retardation of amyloids fibrils formation by nanoparticle effects.