High pressure modulates amyloid formation.
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.
Torrent
Joan
J
INSERM U710, CC 105, Université Montpellier 2, Place Eugène Bataillon, F-34095 Montpellier cédex 5, France.
Balny
Claude
C
Lange
Reinhard
R
D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D006874:Hydrostatic Pressure / Q000009:adverse effects; D011487:Protein Conformation; D017510:Protein Folding
D000682:Amyloid