Amyloidogenic and non-amyloidogenic molten globule conformation of β-lactoglobulin in self-crowded regime

The molecular mechanism responsible of the protein self-assembly involves the interplay of different types of interactions and it remains among the most puzzling problems in biophysics. Here we propose an in situ and in real time spectroscopic approach to investigate the thermal unfolding and aggregation path of β-lactoglobuling protein. Thans to the identification of sensitive spectroscopic markers in the vibrational spectra we are able to distinghuish the two characteristic pathways pursued by the protein during its conformational transition from the folded to the molten globular state, as triggered by the pH conditions.