Molecular basis of taste and sensory perception in food, nutrition and environment
Rational design, sinthesis and structure-activity relationship in taste active compounds. Molecular modelling of ligand-receptor interactions in the GPCR and TRP receptor families. Bioactive compounds in sensing from natural sources; isolation from food plants and traditional food; taste-guided analysis. Taste biodiversity and its biological significance. Nutrient chemosensing. Compounds active on TRP channels: somatosensory perception in humans, animals and invertebrates; applications in pharmaceutical, agri-food and enviroment.
Nuclear Magnetic Resonance studies in the agrifood, pharmaceutical and environmental fields
Study of interactions of oligonucleotides (duplex, triplex and quadruplex) with anti-cancer drugs by 1H and 31P NMR spectroscopy; molecular modeling of ligand-DNA complexes. Structure elucidation of natural products, small peptides and modified oligonucleotides. NMR in solution and solid state in pharmaceutical, agrifood and environmental fields. Application of homo- and heteronuclear NMR and of NMR-imaging to studies on the interaction among biopolymers and between biopolymers and other components in complex mixtures, including nanostructured materials and food systems/products.
Design, synthesis and structure-activity studies of compounds endowed with biological activity
Design, synthesis and structure-activity studies of compounds endowed with biological activity, particularly antifungal, antimicrobial and antitumor compounds. Isolation, purification and structural elucidation of natural products. Total synthesis of pharmacologically active natural compounds and analogues. Design of systems able to drive specific bioactives towards appropriate biological targets and to ensure their selective release.
Development and validation of novel analytical approaches
Development of sustainable and economically viable materials for food safety applications. Micro- and nanoscaled electrochemical sensors, including systems based on micro- and nano-sized emulsions. Advanced statistical methods for analytical chemistry. Applications of non-destructive and non-invasive methodologies (e-nose, e-tongue, image analysis) to agro-food issues.
Development of thermal analysis methodologies
The main methodologies used for thermal analysis (DSC, Knudsen-regimen DSC, Isotermal Titration Calorimetry, thermogravimetry) are applied to materials and issues of relevance to the agro-food, environmental, and pharmaceutical sectors, as well as to the preservation of materials of historical and artistic relevance. Developed applications range from macromolecules and their interactions to binding studies, and from analysis of biological kinetics to conditional stabilization of biopolymers.
Structure-function relationships in proteins
Established and innovative approaches are applied to studies on the structure/function relationship in proteins of various origin, with very diverse biological functions. Investigated protein include: 1) soluble and insoluble food proteins, including food allergens; 2) proteins involved in micronutrient transport and in the assembly/insertion of organic and inorganic cofactors; 3) proteins involved in recognition among species and among cells, as well as in the formation of biofilms; 4) proteins involved in oxidative protection; 5) proteins and peptides involved in regulatory events of physiological and pathological relevance; 6) enzymes of industrial and biotechnological relevance.
Innovative methods for protein structural studies
Spectroscopy-based methodologies (fluorescence, circular dichroism, NMR) have been specifically developed to allow studies on both soluble and insoluble proteins. These methodologies rely on "intrinsic" protein spectroscopic reporters, on the use of selective probes, and on the binding of proteins to appropriately modified nanoparticles. These methodologies are being applied to pursue the following main goals: 1) structural characterization of proteins in their native state and after modification by biotechnological processes (physical, chemical, enzymatic); 2) conditional stability and folding/unfolding studies; 3) structural determinants of the uptake of proteins and peptides by cells and tissues; 3) determinants of the biological function of proteins and peptides; 4) specificity of interaction of proteins with other proteins and with structured and non-structured non-protein components of the system.
This activity relies on a combination of separative, spectroscopic, and immunochemical approaches (including the use of site- and residue-specific probes, of controlled proteolysis, and of suitable bioinformatic tools) to define the relevance of individual protein components in complex systems to biotechnological transformations and to biological activities and. Also addressed is the role of post-translational modifications, of process-induced modifications, and of interactions that occur among proteins and between proteins and other components of the system (including the relevance of the structural state of the proteins and of their interactors).