Website
https://www.dbcf.unisi.it/it/dipartimento/personale/docenti/stefano-mangani

Education
Degree in Chemistry magna cum laude, from University of Florence, March 1977.

Academic positions
Postdoctoral fellow in the Department of Biophysics and Biochemistry at Texas A&M University 1979-1981. Assistant Professor, Chemistry Department, University of Siena 1983-94
Present position
Full professor of General and Inorganic Chemistry, Department of Biotechnology, Chemistry and Pharmacy, University of Siena, 1994 -
Society memberships
Italian Chemical Society, Italian Crystallographic Association, European Crystallographic Association, American Crystallographic Association, Society of Biological Inorganic Chemistry

Scientific Publications
Author/co-author of 187 publications on international scientific journals and book chapters on scientific book series. Author and Editor of the book: “Disruption of Protein-Protein Interfaces, Springer 2013. Depositor of about 140 protein structures in the Protein Data Bank. Depositor of 2 international patents on new inhibitors of human thymidylate synthase.
Total Citations: 3627/3878/4611
H-index: 35/34/38 Scopus (June 2017)/WoS (June 2017)/Google Scholar (June 2017)
Summary of scientific activities
Main field of research: structural biology, enzyme mechanism and bioinorganic chemistry
Research Themes:
1) Study of the catalytic mechanism and of the inhibition of bacterial ?-lactamase enzymes of all classes
?-lactamase enzymes are a major defense system of bacteria against antibiotics and represent a threat for human health since that they confer resistance against ?-lactam antibiotics. Understanding the chemical basis of ?-lactam antibiotics inactivation and how ?-lactamases can be inhibited is the starting point for developing new drugs to treat infections by resistant bacterial strains. The main tool for the study is the determination, by X-ray crystallography, of the tridimensional structure of ?-lactamases and of their complexes with molecules able to provide information about the catalytic pathway.
2) Title: Mechanistic studies on metalloenzyme and metalloprotein function and inhibition.
Proteins and enzymes containing metal cofactors play crucial roles in cellular metabolism. The peculiar chemistry of metal ions is exploited to perform the most difficult chemical reactions. The information coming from crystal structure determination of such proteins and from x-ray absorption spectroscopy coupled to NMR spectroscopy is used to explain at the molecular/atomic level the properties of such systems adding basic knowledge in the perspective of biotechnological applications.
3) Title: Studies on inhibition and regulation of enzymes and proteins involved in cancer, neurodegenerative disorders and neglected diseases.
These studies aim to provide the structural basis for the development of innovative drugs to fight different pathologies. The understanding of protein function and the protein-protein interactions that are involved in metabolic pathways allows to conceive innovative molecules able to regulate such pathways and to contrast the progression of such pathologies. The systems studied are bacterial and human thymidylate sinthase; human Glutaminyl-peptide cyclotransferase (QPCT); peptides involved in Alzheimer disease; pteridine reductase and dual dihydrofolate-thymidylate synthase from Trypanosoma and Leishmania spp.