This chapter attempts to explore protective role of chaperone proteins in the neurodegenerative diseases caused by amyloidosis. These chaperones prevent amyloid pathology either directly, through chemical interactions with amyloidogenic species to mediate their refolding, solubilization and degradation, or indirectly, by scavenging reactive oxygen species produced as by-products of amyloid aggregation. Here we focus on structural and morphological changes during aggregation of amyloids which have been identified using Nuclear magnetic resonance spectroscopy, X-ray crystallography, Electron microscopy, Atomic force microscopy and other biophysical techniques as well as interactions between chaperone proteins and amyloid moieties. Non-proteolytic chaperones mediate amyloid clearance and metabolism through conformational changes due to proximity binding. In this chapter, we delineate these interactions as well as the molecular mechanism of chaperones used to sequester ROS products of amyloidosis with focus on amyloid-β peptides associated with the Alzheimer’s disease.
Part of the book: Amyloid Diseases