Martino Bolognesi
e-mail: martino.bolognesi AT unimi.it
website: users.unimi.it/biolstru/Home.html
affiliation: Dept of Biomolecular Science and Biotechnology
research area(s): Chemical Biology, Computational Biology
Course:
Biomolecular Sciences
University/Istitution: Università di Milano
University/Istitution: Università di Milano
Martino Bolognesi graduated in Chemistry, "cum laude", at the University of Pavia in 1974, and subsequently specialized in Biochemistry (1978, "cum laude"), both as Fellow of Collegio Ghislieri, Pavia. Between 1978 and 1981 he spent his post-doc years at the University of Oregon (USA), Institute of Molecular Biology (Prof. B.W. Matthews) and at the Max Planck Institut fur Biochemie (Martinsried-Munich, Germany, Prof. R. Huber), respectively. Back in Italy, he was Associate Professor of Biophysical Chemistry at the University of Pavia (1981-1991), subsequently, full Professor of Biophysics, at the University of Genova (1991-2004), where he led the bio-crystallographic lab hosted at the Advanced Biotechnology Center, U. of Genova. From Novemberv2004 he is full Professor of Biochemistry at the Dept. of Biomolecular Sciences and Biotechnology, University of Milano, where a new structural biology lab has been established. His scientific career has been constantly centered on the study of protein structure through X-ray crystallography.
Martino Bolognesi"s scientific activity is focused on the application of structural biology and biophysics to the study of protein functionality. To this aim, over the years, his research dealt with heme-proteins, proteases, copper proteins, redox enzymes, viral enyzmes and proteins involved in apoptosis. The methods mainly applied are protein crystallography, protein biochemistry and biophysics (a selection of spectroscopic techniques), small angle X-ray scattering, and computational biology. The use of synchrotron radiation has been a central theme in all the mentioned activities. In recent times (form 2005) the interest for drug design/discovery has grown substantially, considering that several of the protein structures solved in the bolognesi lab are important targets for the design of new molecules that may act as drug leads. In this context, two patents have been recently filed. Prof. Bolognesi trained several students and PhD students over his career (more than 30). Some of them (3) cover currently relevant positions in Europe, at research centers and at synchrotron sites. Others (7), cover permanent positions in Italy as Full- or Associate-Professors and University researchers a in different Universities or in national research institutions.
Nuccitelli, A., Cozzi, R., Gourlay, L. J., Donnarumma, D., Necchi, F., Norais, N., Telford, J.
L., Rappuoli, R., Bolognesi, M., Maione, D., Grandi, G. & Rinaudo, C. D. From the Cover:
Structure-based approach to rationally design a chimeric protein for an effective vaccine
against Group B Streptococcus infections. Proc Natl Acad Sci U S A 108, 10278-83.
Ricagno, S., Pezzullo, M., Barbiroli, A., Manno, M., Levantino, M., Santangelo, M. G., Bonomi, F. &
Bolognesi, M. (2010). Two latent and two hyperstable polymeric forms of human neuroserpin. Biophys J 99,
3402-11.
Pesce, A., Nardini, M., Dewilde, S., Capece, L., Marti, M. A., Congia, S., Salter, M. D., Blouin, G. C., Estrin,
D. A., Ascenzi, P., Moens, L., Bolognesi, M. & Olson, J. S. (2010). Ligand migration in the apolar tunnel of
cerebratulus lacteus mini-hemoglobin. J Biol Chem.
Barbet-Massin, E., Ricagno, S., Lewandowski, J. R., Giorgetti, S., Bellotti, V., Bolognesi, M., Emsley, L. &
Pintacuda, G. (2010). Fibrillar vs crystalline full-length beta-2-microglobulin studied by high-resolution solid
state NMR spectroscopy. J Am Chem Soc 132, 5556-7.
Cossu, F., Milani, M., Mastrangelo, E., Vachette, P., Servida, F., Lecis, D., Canevari, G., Delia, D., Drago, C., Rizzo, V., Manzoni, L., Seneci, P., Scolastico, C. & Bolognesi, M. (2009). Structural basis for bivalent smac-mimetics recognition in the IAP protein family. J Mol Biol 392, 630-44.
L., Rappuoli, R., Bolognesi, M., Maione, D., Grandi, G. & Rinaudo, C. D. From the Cover:
Structure-based approach to rationally design a chimeric protein for an effective vaccine
against Group B Streptococcus infections. Proc Natl Acad Sci U S A 108, 10278-83.
Ricagno, S., Pezzullo, M., Barbiroli, A., Manno, M., Levantino, M., Santangelo, M. G., Bonomi, F. &
Bolognesi, M. (2010). Two latent and two hyperstable polymeric forms of human neuroserpin. Biophys J 99,
3402-11.
Pesce, A., Nardini, M., Dewilde, S., Capece, L., Marti, M. A., Congia, S., Salter, M. D., Blouin, G. C., Estrin,
D. A., Ascenzi, P., Moens, L., Bolognesi, M. & Olson, J. S. (2010). Ligand migration in the apolar tunnel of
cerebratulus lacteus mini-hemoglobin. J Biol Chem.
Barbet-Massin, E., Ricagno, S., Lewandowski, J. R., Giorgetti, S., Bellotti, V., Bolognesi, M., Emsley, L. &
Pintacuda, G. (2010). Fibrillar vs crystalline full-length beta-2-microglobulin studied by high-resolution solid
state NMR spectroscopy. J Am Chem Soc 132, 5556-7.
Cossu, F., Milani, M., Mastrangelo, E., Vachette, P., Servida, F., Lecis, D., Canevari, G., Delia, D., Drago, C., Rizzo, V., Manzoni, L., Seneci, P., Scolastico, C. & Bolognesi, M. (2009). Structural basis for bivalent smac-mimetics recognition in the IAP protein family. J Mol Biol 392, 630-44.
Project Title:
Structure-based search for drug leads for the development of antivirals or of pro-apoptotic compounds (and other targets)
We apply computational biology, biophysical, biochemical and X-ray crystallography methods to search for new low molecular weight molecules able to inhibit specific protein components of different biochemical processes. In the case of RNA viruses, we aim at interfering with the enzymes involved in viral replication to halt viral infection. More specifically, we target helicases and RNA-dependent RNA-polymerases of Dengue, Yellow fever, West Nile and related viruses. In the field of pro-apoptotic drugs, to be used in cancer therapy, we target Inhibitor of Apoptosis Proteins (IAPs) through the development of peptide-mimetic compounds. According to the stage of project development, we apply in silico search of compound libraries, docking methods, biophysical approaches, biochemical characterization of recombinant protein/enzyme samples, and, for most targets, we study protein 3D structures through X-ray crystallography. Such combined approach is state of the art, being endowed with a strong discovery potential, and lends itself to practical applications and international collaborations. Both projects are continuously active and supported by national/international grants.
The lab is running other related projects based on the structural biology and biophysics approaches mentioned above. Targets of such additional projects are antigen structure and vaccine development, protein misfolding processes, and transcription factor structure. Each of these is available for a PhD project over the next three years.
The lab is running other related projects based on the structural biology and biophysics approaches mentioned above. Targets of such additional projects are antigen structure and vaccine development, protein misfolding processes, and transcription factor structure. Each of these is available for a PhD project over the next three years.