Dr Caterina Alfano received her Master’s Degree in Chemistry (curriculum in chemical biology) with full marks and honours (110/110 summa cum laude) at the University Federico II of Naples (Italy) in 2002. She then received her PhD Degree in 2006, with a thesis on “Studies of protein/nucleic acids interactions by Nuclear Magnetic Resonance” gaining a solid expertise in structural biology and biophysics applied to macromolecules. The research activity was carried out at the Biophysics Laboratories – School of Biological Sciences – University of Portsmouth (UK) under the supervision of Prof C. Crane-Robinson, and at the Randall Division of Cell and Molecular Biophysics – King’s College of London (UK) under the supervision of Prof MR. Conte. Of note, the research led to the discovery of the “La module” of La protein as a novel RNA-binding module. Later, the La module was found conserved across other RNA binding proteins, today known as La-Related Proteins (LaRPs).
In 2017, Caterina joined Ri.MED after several years spent in well-recognized international research institutes such as King’s College London (UK), IRBM Merck Sharp & Dohme (Italy), CIC-Biogune (Spain), and MRC National Institute for Medical Research (UK), later merged in the Francis’s Crick Institute (UK).
Of note, Caterina’s career trajectory combines experience in traditional academic settings and in industrial pharma sector, putting her in the distinctive position of understanding both basic and translational research in a world where a closer integration between these two sectors is required to push forward innovation and generate competitive Science.
Today, Caterina is the Head of the Structural Biology and Biophysics Unit of Ri.MED, member of both the Research & Development Coordination Committee and the Gender Equality Plan Committee of Ri.MED

The main emphasis of Caterina’s research is the understanding of the complexities of macromolecular structure, function and interactions, with particular focus on biomolecular systems linked to neurodegenerative diseases. More specifically, Caterina’s research activities aim at providing biophysical and structural information on biological phenomena guided by folding, phase transition and interaction of proteins and protein complexes with the ultimate goals of understanding the molecular mechanisms underlying serious neurodegenerative pathologies. The research relies on the concept that knowledge of the normal function and of the interaction network of aggregating proteins is a key tool to design molecules which can specifically compete out pathological aggregation. Native interactions could indeed provide important means of altering and controlling the function and assembly of proteins involved in neurodegenerative diseases, and could fulfil a protective role against aberrant aggregation.
In parallel, Caterina is interested in the structural and biophysical characterization of Mussel Foot adhesive proteins (Mfps), which, similarly to proteins involved in neurodegenerative diseases, undergo to phase transition and form stable protein liquid droplets and aggregates. The understanding of the molecular basis of the adhesive proprieties of Mfps could indeed be crucial for the developing of nature-inspired bioadhesives able to work in wet environment, for which there is a growing interest for biomedical applications in several areas as tissue engineering, implantation of medical devices and wound closure.

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