High pressure research vol:22 issue:3-4 pages:733-736
Protein folding or unfolding can lead to the population of intermediates or partially unfolded conformations that have a high aggregation tendency. Some of these states associate in vivo to form fibrillar structures. These fibrils are the hallmark of molecular diseases such as Alzheimer's disease. It has been suggested that in vitro fibril formation is a generic property of all proteins. Insulin has been chosen as a model protein to study the process of fibrillation with Fourier-transform infrared spectroscopy. It is found that the formation of fibrils is preceded by amorphous aggregation. We also investigated the effect of hydrostatic pressure on insulin fibrils. The observed spectral changes are interpreted in terms of fibril dissociation into protofilaments, Preliminary results indicate that pressure is an interesting tool to characterize the interactions that maintain the fibril structure.