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How is function encoded in protein self-assembly?
In our laboratory, we study the mechanisms at the basis of protein self-assembly in solution and how they regulate biological processes. Such knowledge allows us to interact both with academic and industrial collaborators and have impact in both of these areas.

We focus on two main areas of interest, but any challenge that involves biophysical chemistry and biomolecular interactions spurs our curiosity and efforts!

1. Protein self-assembly proteins shape lipid membranes to maintain cellular compartmentalisation.

Compartmentalisation of chemical reactions is fundamental for the function of any biological cell. The confinement provided by membrane interfaces in intracellular organelles allows their contents to carry out specific tasks without the interference from other processes. Specifically, we focus on the biochemical and biophysical mechanisms of cellular membrane repair. Remodelling of phospholipid membranes underpins most cellular functions from membrane trafficking to viral infections and genome compartmentalisation.

Scientific Questions we are addressing –
•    What are the signals that lead proteins to assemble into larger structures to sculpt phospholipid membranes?
•    How does membrane integrity maintain the healthy state of a biological cell?
•    Can we repurpose these biological processes for novel functions?

We tackle these questions with a combination of biochemistry, cell biology and protein design approaches.

2. The physical chemistry that governs protein physical status in solution

We collaborate with industry partners to understand how to combine knowledge of of protein-protein interactions with the development of specific biophysical/analytical methodologies to support prediction and faster optimisation of formulations. Such knowledge is crucial also for academics that study protein aggregation in the context of healthy and diseased states.

We tackle this challenge with a combination of biophysical and analytical chemistry techniques and structural biology approaches.

Our lab has expertise in:

• Protein engineering and high-level recombinant peptide and protein expression for structural studies
• De novo and rational design of peptides and proteins
• Protein stability and protein-protein interaction measurements
• Characterisation of self-assembly and aggregation of proteins
• Characterisation of protein-membranes interactions
• Mechanisms of nuclear envelope membranes repair
• Endosomal membrane trafficking