The research aims at determining the three-dimensional structure of complex biological systems, for example the conformational state of macromolecules, mainly proteins, through the use of nuclear magnetic resonance (NMR) spectroscopy techniques. Furthermore, it relates the structural information thus collected with the chemical properties of the molecules so far studied, including the ability to bind metal ions and other small molecules and, in general, the interactions between different chemical species. The process of rationalization of the observed properties and of adaptation to simplified and general models, occurs through advanced methods of multivariate analysis of high resolution spectroscopic data collected with the spectrometer operating at 600MHz available to the group. The same approach is used in metabolomics, ie in the comparison of molecular profiles or patterns of metabolites of biological systems (eg tissues or foods). Therefore a holistic view of the biological system is constructed, which allows a more complete and comparative evaluation of the anisotropic distribution of molecules in heterogeneous systems.
Over the years, research has included the study of calcium-binding proteins belonging to the superfamily of the EF-hand proteins. This particular class of macromolecules is the basis of a considerable number of biological processes including muscle contraction, cascade activation of enzymes, the opening of ion channels and in general all the mechanisms in which the calcium ion transmits signals for the cellular function even to determine the moment of death. The study of these functions requires different complementary competences existing within the research group: design of genetic material to be introduced, using molecular biology techniques, within selected bacteria; cultivation of micro-organisms to over-express proteins of interest at high concentrations; acquisition of nuclear magnetic resonance spectra for the resolution of the three-dimensional structure; extraction of information on the relationship between structure and biological function. The complexity of spectroscopic and structural information is reduced through translation into simplified descriptors that have been developed by the group and which derive from the multivariate analysis of the observed data.
The skills acquired on the analysis of spectroscopic data of complex molecules such as proteins has prompted the research group to be interested, for several years, also in problems of definition and simplification of molecular profiles of biological systems complicated by the presence of supra-molecular structures.
To this end, the group applies the principles of metabolomics for the classification of transformation phenomena occurring in the biological matrix (eg food) due to technological processes or differences in production methods. In particular, the research group uses the molecular profiles emerging from the NMR spectra of a studied food (for example GMO) for comparison with conventional control groups. This is why the group is able to provide the study with a holistic view rather than defining the system through the observation of a small pool of selected molecules based on preconceived ideas. Currently, the comparisons between GMO plant species and between different methods of breeding of fish species is under way. The observation of molecular interactions through NMR spectroscopy is the basis of current studies on the relationship between the food matrix structure and the effects of simulated in vitro digestion.
