Scientific Interests: The main objective of our work is the understanding the molecular bases of protein aggregation. Specific human proteins loose their native fold and eventually deposit as amyloid fibrils and other kinds of polymers. Such aggregation is responsible for several severe and incurable human pathologies. We employ several structural biology techniques (X-ray crystallography, NMR and Cryo electron microscopy, SAXS) and many biophysical methods to characterise the structure, dynamics and fold stability of native and aggregated conformations. This effort not only should contribute to understand the biochemical/ biophysical mechanisms underlying protein aggregation, but ultimately aims at identifying anti-aggregation strategies to treat patients affected by misfolding diseases.
The project focuses on the structural characterisation of TDP-43 whose aggregation is one of the main triggers of ALS. Funded in 2017.
The project aims at understanding the molecular bases of the toxicity and aggregation propensity of light chains in the context of AL amyloidosis. Funded in 2016.
In this project we are trying to understand the mechanism of polymerisation and the structure of resulting neuroserpin polymers, in order to identifiy efficient inhibitors. Funded in 2016 and in 2011.
This project aims to set understand the bases of beta-2 microglobulin amylodi propensity: protein dynamics, structure and sequence based properties. Funded in 2010