Research Activity

After the genomic revolution the focus of biological research is shifting from the description of singular interactions between macromolecular compounds, to the comprehensive detection, measurement and mapping of complex functional biomolecular systems. To achieve this task we are interested in developing and applying new technologies in the fields of mass spectrometry and proteomics. We choose mass spectrometry as the principal analytical tool as this technique is, up to now, the most sensitive and specific tool for protein microanalysis. Our group is mainly interested in the development and application of sensitive and specific methods for protein identification and microcharacterization. In particular, we are developing novel approaches that can be applied to proteome analysis of cells under physiological and pathological states.

Our laboratory, established under the sponsorship of FIRC (Federazione Italiana Ricerca sul Cancro, http://www.airc.it/sito/firc/indexfirc.html) and IFOM (FIRC Institute of Molecular Oncology, http://www.ifom-firc.it/), has state of the art equipment for protein microanalysis and identification, including a MALDI-TOF, a Nano electrospray Q-TOF and a Ion trap mass spectrometer.

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Ion Trap
Current projects within the lab focus on two critical areas with the field of proteomics: protein-protein interactions and post-translational modifications analysis. For a systematic analysis of networks of  protein-protein interactions we are making  use of specific purification methodologies, such as double epitope tagging or immunoprecipitation techniques, that allow the simultaneous purification of all protein partners and their identification by mass spectrometry.


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Maldi-TOF
Post-translational modification (PTM) of proteins is a key event in several cellular processes as signaling, metabolism and targeting and is, at the end, responsible of the correct protein activity. We have developed specific and sensitive methods for the enrichment and the isolation of phosphorylated peptides present in ‘in gel’ separated proteins that allow us to identify and localize the site of modification. Another field of interest of our lab is the  assessment of the oxidative status of cysteine residues. We have recently developed a new method, based on in gel digestion, on target reduction and alkylation of the cysteine residues and on MALDI-TOF MS, that allows the rapid and sensitive characterization of cysteine containing proteins and assignement of disulfide bonds. This procedure is very rapid, efficient, sensitive and suitable for determining the presence of disulfide bonds and the native cysteine pairings, thus increasing the structural information related to a protein oxidative state for proteomics studies.

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