Protein folding, misfolding and aggregation in vitro and in situ studied by biophysical approaches, including infrared spectroscopy and microspectroscopy, optical spectroscopy (absorption, florescence, circular dichroism), and mass spectrometry. Major research topics: 1) protein stability; 2) amyloid aggregation; 3) structure-function relation; 4) aggregation of recombinant proteins; 5) protein-protein and protein-ligand interactions; 6) nano- and bio-materials.
Monitoring of biological processes in situ, mainly by means of FTIR (micro)spectroscopy, with particular interest in the role of bioactive lipids in different cell processes, including differentiation, maturation, stress response, protein misfolding.
Ami Diletta – PostDoc Fellow room 4051/4050, IV floor , building U3 tel: +39 02 6448 3461/3459 firstname.lastname@example.org
Natalello, A., Mangione, P., Giorgetti, S., Porcari, R., Marchese, L., Zorzoli, I., et al. (2016). Co-fibrillogenesis of wild-type and D76N β2-microglobulin: The crucial role of fibrillar seeds. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 291(18), 9678-9689. Dettaglio
Konijnenberg, A., Ranica, S., Narkiewicz, J., Legname, G., Grandori, R., Sobott, F., et al. (2016). Opposite Structural Effects of Epigallocatechin-3-gallate and Dopamine Binding to α-Synuclein. ANALYTICAL CHEMISTRY, 88(17), 8468-8475. Dettaglio
Ami, D., Lavatelli, F., Rognoni, P., Palladini, G., Raimondi, S., Giorgetti, S., et al. (2016). In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study. SCIENTIFIC REPORTS, 6, 29096. Dettaglio
Ami, D., Mereghetti, P., Foli, A., Tasaki, M., Milani, P., Nuvolone, M., et al. (2019). ATR-FTIR Spectroscopy Supported by Multivariate Analysis for the Characterization of Adipose Tissue Aspirates from Patients Affected by Systemic Amyloidosis. ANALYTICAL CHEMISTRY, 91(4), 2894-2900. Dettaglio
Tedeschi, G., Mangiagalli, M., Chmielewska, S., Lotti, M., Natalello, A., & Brocca, S. (2017). Aggregation properties of a disordered protein are tunable by pH and depend on its net charge per residue. BIOCHIMICA ET BIOPHYSICA ACTA, 1861(11), 2543-2550. Dettaglio