Research
Our work sits at the interface between enzymology, biophysics and prebiotic chemistry.
We ask how compartments without membranes shape chemical reactivity (in living cells today, and possibly at the origin of life) and how the same principles can be used to redesign enzymes for medicine.
Condensates as prebiotic microreactors
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Nucleotides and short RNA fragments form membrane-less droplets through liquid-liquid phase separation. We characterise how these droplets assemble, how stable they are across pH and temperature, and how the dense phase differs from bulk solution in its ability to concentrate reactants and tune reaction rates. Chemistry that is unproductive in dilute solution can proceed inside them, which makes them attractive candidates for primitive, membrane-less microreactors.
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Enzymes in crowded and phase-separated environments
Enzymes almost never operate in dilute buffer. In the cell they work in crowded, compartmentalised surroundings. We reconstruct phase-separated systems that partition enzymes into a dense phase and sustain their activity over long timescales, then measure how crowding, viscosity and restricted diffusion reshape catalysis. This lets us connect the behaviour of an enzyme in a test tube to how it might actually function inside a living cell, and to design compartments that keep enzymes active and stable for biotechnological use. This line grew out of work carried out at OIST and continues in Perugia.
Dopamine, serotonin and PLP-dependent enzymes
DOPA decarboxylase (AADC) is the pyridoxal 5′-phosphate-dependent enzyme that produces dopamine and serotonin from their amino acid precursors. For most of its history it has been treated as a constitutive downstream step, but its regulation and evolution are far less understood than its basic chemistry. We study how the enzyme is controlled by its molecular environment, and how the enzyme family has evolved.
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Protein engineering
We use directed evolution and rational design to reshape enzymes with therapeutic and biotechnological potential. By engineering activity, stability and resistance to harsh conditions, we build enzymes that can function where natural ones fail or are highly inefficient.