2007 Volume 17 Issue 1 Pages 42-49
Pressure is an important perturbant applied in studies of folding and unfolding of globular proteins. Recently, the application of this perturbant has been extended to the study of amyloid fibrils, which will be reviewed here. The effects of pressure on amyloid fibrils seem various, being positive or negative, dependent on the protein species and experimental conditions. Several reports have shown that pressure drives the formation of amyloid fibrils via pressure-induced unfolded structure of proteins. In contrast, there are also several studies showing the pressure-induced depolymerization of amyloid fibrils, suggesting the deficient packing and/or hydration in the fibril structure. Furthermore, a novel adaptation or maturation phenomenon has been found under pressurized conditions, demonstrating the structural diversity of amyloid fibrils, one of unique features which cannot be predicted with Anfinsen's dogma.
