The research focuses on the molecular mechanisms through which metals and protein structural disorder regulate protein function, interactions, and cellular processes, with particular attention to their implications for human health.
- Nickel, intrinsically disordered proteins, and carcinogenesis. A major research area focuses on the molecular mechanisms linking exposure to nickel compounds to lung carcinogenesis. The aim is to understand how nickel interferes with proteins and cellular processes involved in stress responses and tumor progression, in order to identify new potential targets for biomedical intervention. Particular attention is devoted to NDRG1, a protein involved in tumor progression and characterized by an intrinsically disordered region. Its structural properties, molecular interactions, and modulation by metals are investigated. NDRG1 also serves as a model for understanding the role of intrinsically disordered regions in pathological processes and for exploring new strategies for their pharmacological modulation.
- Metal homeostasis and metalloprotein maturation. A second research area concerns the molecular mechanisms regulating transition-metal homeostasis, with particular emphasis on nickel. These studies address the processes controlling metal recognition, transport, distribution, and selective incorporation into proteins. A model system is the maturation of urease, a nickel-containing metalloenzyme that requires a network of accessory proteins responsible for metal acquisition and insertion into the active site. Structural and functional studies of these proteins help clarify the molecular principles that ensure selectivity and efficiency in protein metallation. These topics are investigated in both prokaryotic and eukaryotic systems, with the broader aim of understanding how alterations in metal homeostasis and metal-protein interactions contribute to pathological processes and may provide new therapeutic strategies.
