Aggregation States of Aβ1–40, Aβ1–42 and Aβp3–42 Amyloid Beta Peptides: A SANS Study

Aggregation states of amyloid betapeptides for amyloid betaA β 1 – 40 to A β 1 – 42 and A β p 3 – 42 are investigated through small angle neutron scattering(SANS). The knowledge of these small peptides and their aggregation state are of key importance for the comprehension of neurodegenerative diseases (e.g., Alzheimer’s disease). The SANS technique allows to study the size and fractal nature of the monomers, oligomersand fibrils of the three different peptides. Results show that all the investigated peptides have monomers with a radiusof gyrationof the order of 10 A, while the oligomersand fibrils display differences in size and aggregation ability, with A β p 3 – 42 showing larger oligomers. These properties are strictly related to the toxicity of the corresponding amyloidpeptide and indeed to the development of the associated disease.