Dr. Emilio Parisini
In the Biotechnology lab, we carry out structure-function relationship studies on different biological systems using molecular biology, biochemistry, biophysics and X-ray crystallography techniques. Our research interests are mostly at the interface between chemistry and biology and they focus primarily on the study of the interactions between proteins and their ligands, substrates or inhibitors. In particular, we investigate the functional and the structural properties of members of the cadherin family of cell adhesion proteins and of several different enzymes for diagnostic and therapeutic applications.
Dr. Emilio Parisini’s scientific background is in molecular biology, structural biology and solid-state chemistry. He received a Ph.D. in Chemistry from the University of Bologna (Italy) in 1995 and carried out post-doctoral research at the Universities of Göttingen (Germany, 1995–1997), Cambridge (U.K., 1997–2001) and Harvard (U.S.A., 2001–2009). In 2008, he also obtained a M.Sc. in Epidemiology from Harvard University. From 2010 to 2019, he was a Group Leader at the Center for Nano Science and Technology of the Italian Institute of Technology in Milano (Italy). In 2019, he became Principal Investigator (ERA-chair holder) at the Latvian Institute of Organic Synthesis.
Selected recent publications
- Brullo C, Rapetti F, Abbate S, Prosdocimi T, Torretta A, Semrau M, Massa M, Alfei S, Storici P, Parisini E, Bruno O. Design, synthesis, biological evaluation and structural characterization of novel GEBR library PDE4D inhibitors. Eur. J. Med. Chem. 2021, 223, 113638.
- Rigoldi, F.; Donini, S.; Torretta, A.; Carbone, A.; Redaelli, A.; Bandiera, T.; Parisini, E.; Gautieri, A. Rational backbone redesign of a Fructosyl Peptide Oxidase to widen its active site access tunnel. Biotechnol. Bioeng. 2020, 117, 3688.
- Torretta, A.; Lopez-Cara, L.C.; Parisini, E. Crystal structure of the apo and the ADP-bound form of choline kinase from Plasmodium falciparum. Crystals, 2020, 10, 613.
- Vettraino, C.; Peracchi, A.; Donini, S.; Parisini, E. Structural characterization of the human O-phosphoethanolamine phospho-lyase. Acta Crystallogr. Sect F, 2020, F76, 160.
- Cavalloro, V.; Russo, K.; Vasile, V.; Pignataro, L.; Torretta, A.; Donini, S.; Semrau, M. S.; Storici, P.; Rossi, D.; Rapetti, F.; Brullo, C.; Parisini, E.; Bruno, O.; Collina, S..Insight into GEBR-32a: chiral resolution, absolute configuration and enantiopreference in PDE4D inibition. Molecules 2020, 25, 935.
- Dalle Vedove, A.; Falchi, F.; Donini, S.; Dobric, A.; Germain, S.; Di Martino, G. P.; Prosdocimi, T.; Vettraino, C.; Torretta, A.; Cavalli, A.; Rigot, V.; Andre’, F.; Parisini, E. Structure-based virtual screening allows the identification of efficient modulators of E-cadherin-mediated cell-cell adhesion. Int. J. Mol. Sci. 2019, 20, 3404.
- Prosdocimi, T.; Mollica, L.; Donini, S.; Semrau, M. S.; Lucarelli, A. P.; Aiolfi, E.; Cavalli, A.; Storici, P.; Alfei, S.; Brullo, C.; Bruno, O.; Parisini, E. Molecular bases of PDE4D inhibition by memory-enhancing GEBR-library compounds. Biochemistry 2018, 57, 2876.
- Rigoldi, F.; Donini, S.; Giacomina, F.; Sorana, F.; Redaelli, A.; Bandiera, T.; Parisini, E.; Gautieri, A. Thermal stabilization of the deglycating enzyme Amadoriase I by rational design. Sci. Rep. 2018, 8, 3042.
- Nardone, V.; Lucarelli, A. P.; Dalle Vedove, A.; Fanelli, R.; Tomassetti, A.; Belvisi, L.; Civera, M.; Parisini, E. Crystal structure of human E-cadherin-EC1EC2 in complex with a peptidomimetic competitive inhibitor of cadherin homophilic interaction. J. Med. Chem. 2016, 59, 5089.
- Rigoldi, F.; Gautieri, A.; Dalle Vedove, A.; Lucarelli, A. P.; Vesentini, S.; Parisini, E. Crystal structure of the deglycating enzyme Amadoriase I in its free form and substrate-bound complex. Proteins 2016, 84, 744.
- Dalle Vedove, A.; Lucarelli, A. P.; Nardone, V.; Matino, A.; Parisini, E. The X-ray structure of human P-cadherin EC1-EC2 in a closed conformation provides insight into the type I cadherin dimerization pathway. Acta Crystallogr., Sect. F, 2015, F71, 371.