The potential of Fourier Transform Infrared (FTIR) Spectroscopy for the study of protein aggregation

by Prof. Silvia Maria Doglia (Dipartimento di Biotecnologie e Bioscienze Università di Milano Bicocca)

Thursday 13 May 2010, 15:00 → 16:00 Europe/Rome

Aula 8 (Dipartimento di Fisica - Ed. E. Fermi)

Protein aggregation is a complex process that plays a crucial role in medical sciences and biotechnology. Degenerative diseases such as Alzheimer, Parkinson and prion disorders are characterized by the presence in tissues of amyloid protein aggregates, which can lead to cell death. In biotechnology, aggregation occurs in the form of inclusion bodies (IBs) during the overexpression of recombinant proteins in microbial cells. FTIR appears to be well-suited to study protein aggregation, since a specific infrared response characterizes the protein-protein β-sheet interaction in amyloid aggregates as well as in IBs that could be useful model systems to study in vivo protein aggregation (1,2). The FTIR approach will be illustrated taking as an example the amyloid protein ataxin3 (AT3) and its inclusion bodies formed during the AT3 recombinant expression in E.coli. The kinetics of aggregation and the structural properties of aggregates monitored by FTIR will be also presented for a model prion peptide (3).