Amyloid fibril formation from human and bovine serum albumin followed by quasi-simultaneous Fourier-transform infrared (FT-IR) spectroscopy and static light scattering (SLS).

Human and bovine serum albumins are widely known proteins that can form amyloid fibrils under destabilizing conditions. Use of well-known proteins with easily-controlled aggregation process, and comparison of these processes for similar proteins from different species, could help elucidate the nature of the aggregation process implicated in many degenerative diseases, for example Alzheimer's, Parkinson's, or type II diabetes. In this work both amyloidogenic mechanisms have been studied by use of infrared spectroscopy in combination with static light scattering, enabling analysis of intra and intermolecular processes and measurement of prefibril and fibril growing quasi-simultaneously. Deeper insight into the rearrangements of the secondary structure of the proteins concomitant with the aggregation process has also been gained by mathematical analysis of the infrared spectra by two-dimensional correlation spectroscopy (2DCOS).