Title:Protein Amyloidogenesis Investigated by Small Angle Scattering
VOLUME: 22 ISSUE: 26
Author(s):Caterina Ricci, Francesco Spinozzi, Paolo Mariani and Maria Grazia Ortore
Affiliation:Department of Environmental and Life Science, Faculty of Science, Polytechnic University of Marche, Ancona, Italy.
Keywords:Amyloid, synuclein, SAXS, SANS, scattering, self-assembly.
Abstract:In the last decades, the study of the mechanisms inducing amyloid fibril formation
has involved several experimental and theoretical biophysical approaches. Many efforts
have been made by scientist at the borderline between biology, chemistry, biochemistry and
physics in order to understand why and in which way a protein starts its amyloidogenic pattern.
This fundamental research issue is evolving in parallel to the development of drugs
and inhibitors able to modify protein self assembly towards amyloid fibrils. Small angle xray
and neutron scattering experiments represent suitable methods to investigate protein
amyloidogenesis and the possible effects of inhibitors: they are in-solution techniques, require
low amount of sample and their time-resolution makes it possible to follow aggregation
pattern. In this paper we review small angle x-ray and neutron scattering studies dedicated
to investigate amyloid β peptide and α-synuclein, related to Alzheimer's and Parkinson's
diseases, respectively, together with some other studies that introduced innovative
models to describe with small angle scattering techniques amyloid fibrillation processes.
