Pressure-Temperature Effects on Proteins: Unfolding, Aggregation and Fibrillogenesis

摘要

Several pharmaceutical, medical and food processing problems require a thorough understanding of the protein aggregation mechanism and fibrillogenesis. Here we show that hydrostatic pressure can give information on 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 β-sheet.