Journal of physics-condensed matter vol:14 issue:44 pages:11477-11484
Pressure-induced unfolding of proteins in solution shows analogies to the pressure-induced amorphization observed in some inorganic and polymer systems. More specifically, pressure gives rise to conformations that show a strong tendency to form supramolecular aggregates that have some relevance to molecular diseases. Hydrostatic pressure can tune the conformation of the intermediates along the unfolding/aggregation pathway. Pressure can also be used to probe the stability of the aggregate, and thus the interactions that are responsible for it. In particular, we demonstrate that pressure might be an interesting tool to study the fibril formation. Fourier transform infrared spectroscopy reveals the presence of fibril secondary structures other than random coil and intermolecular beta-sheet.