Lorenzo Soini
I was born in Rovereto, a small town surrounded by mountains in the north of Italy, in 1989. I moved then to Padova where I obtained the Bachelor and the Master Degree in Chemistry. During my studies I also joined the Erasmus Programme that I spent at the “Insituto Superior Tecnico” in Lisbon, Portugal in 2013.
I have started to develop general interest on protein-protein interactions during my Master Degree experimental project in which I performed structural studies on the anti-apoptotic protein Bcl-xL exploiting mainly single-crystal X-ray protein crystallography.
After graduation I decided to go further with a Phd experience. Since September 2016 I am part of the TASPPI European Training Network in which I have found a great opportunity to develop and extend my professional and personal skills.
Project topic: Structural and biophysical characterization of the interactions at the interface between 14-3-3 PPIs and small-molecule stabilizers.
Targeted stabilization with small molecules is a type of modulation of PPIs that has not been followed systematically in the past. However, the advantages provided by the PPIs stabilizers like their high specificity and uncompetitive nature makes it a very innovative and promising approach for drug discovery.
14-3-3 proteins are a family of ubiquitous adaptor proteins involved in multiple processes running in the cell. As adaptor proteins they modulate the enzymatic activity, the subcellular localization and the ability to bind other partner of the proteins that they directly bind.
The project will focus on the identification of small-molecule stabilizers of the 14-3-3 PPIs with the partners BLNK (B-cell linker protein) and SLP76 (Lymphocyte cytosolic protein 2), adaptor proteins modulating signaling downstream B-cell receptors and T-cell receptors respectively.
In order to achieve this goal, a set of biophysical techniques (SPR, FP, ITC, …) orthogonally combined with single-crystal X-ray crystallography will be exploited.