Research Group: Vittorio Bellotti, Patrizia Mangione, Sofia Giorgetti, Sara Raimondi, Francesca Lavatelli, Loredana Marchese, Guglielmo Verona

The research strategy of this group aims to elucidate the molecular events driving, in vivo, the conversion of soluble globular proteins into a insoluble polymeric fibrils.
We have a strong medical and biological background and a long tradition on studying amyloid diseases. See our web site for further details <http://www.amyloidresearch.it>. A PhD student will have the possibility to choose different specific projects:
1. Biochemical characterization of structural events occurring in vitro along the fibrillar transition.
2. Characterization of the biological events occurring in the C. elegans expressing amyloid proteins, focusing on protein aggregation, multisystem effects and changes in metabolic and proteomic profile caused by such aggregates.
3. Discovery of new inhibitors of proteins amyloidogenesis. This last project is mostly based on a stable and strong collaboration with the National Amyloidosis Centre (NAC) of London UK where some of us (Bellotti and Verona) have official positions. Students have the possibility to spend part of their research activity at NAC in UK. In particular, our long-term NAC based activity have led to identification of promising new small molecules and we are running a program of drug discovery focused on the identification of small molecules suitable for the inhibition of the amyloid transition of human transthyretin and the characterization of novel antibodies for the therapy of amyloidosis.

Recent Publications:

• Verona G, Raimondi S, Canetti D, Mangione PP, Marchese L, Corazza A, Lavatelli F, Gillmore JD, Taylor GW, Bellotti V, Giorgetti S. Degradation versus fibrillogenesis, two alternative pathways modulated by seeds and glycosaminoglycans. Protein Sci. 2024 Mar;33(3):e4931. doi: 10.1002/pro.4931
• Raimondi S, Faravelli G, Nocerino P, Mondani V, Baruffaldi A, Marchese L, Mimmi MC, Canetti D, Verona G, Caterino M, Ruoppolo M, Mangione PP, Bellotti V, Lavatelli F, Giorgetti S. Human wild-type and D76N β2-microglobulin variants are significant proteotoxic and metabolic stressors for transgenic C. elegans. FASEB Bioadv. 2023 Oct 25;5(11):484-505. doi: 10.1096/fba.2023-00073. eCollection 2023 Nov
• Lavatelli F, Mazzini G, Ricagno S, Iavarone F, Rognoni P, Milani P, Nuvolone M, Swuec P, Caminito S, Tasaki M, Chaves-Sanjuan A, Urbani A, Merlini G, Palladini G. Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis. J Biol Chem. 2020;295:16572-16584