Title: High Pressure Modulates Amyloid Formation
Volume: 13
Issue: 3
Author(s): Joan Torrent, Claude Balny and Reinhard Lange
Affiliation:
Keywords:
Amyloid, high pressure, fibrils, protein aggregation, protein folding, protein conformation, prion
Abstract: A common mechanism of conformational changes and pathological aggregation of proteins associated with amyloid diseases remains to be proven. High pressure is emerging as a new strategy for studying aspects of amyloid formation. Pressure provides a convenient means to populate and characterize partially folded states, which are thought to have a key role in assembly processes of proteins into amyloid fibrils. High pressure can also be used to dissociate aggregates and amyloid fibrils or on the opposite to generate such species.
