POSITION Associate Professor 2020-current
Scuola of SMFN, Chemistry department “Ugo Schiff”
and CERM
University of Florence, Florence, Italy
Permanent Research Scientist 2007- 2020
EDUCATION International Ph.D. in Structural Biology 2001 – 2004
CERM
Laurea in Chemistry 1995 – 2000
Graduated Cum Laude (110/110)
RESEARCH EXPERIENCE
Current Research Activity, CERM, University of Florence, Florence, Italy 2007 – Current
(See: RESEARCH INTERESTS)
Post doctoral Research, CERM, University of Florence, Florence, Italy 2004 – 2007
Supervisor: Prof. I. Bertini
Title: Structural Genomics di metalloproteine rilevanti per la salute dell’uomo
Summary:The research activity was devoted to characterize metalloproteins involved in severe pathologies, to understand why disease-causing mutations, which occur in proteins, could be pathogenic. In particular the solution structures and dynamics on various time scales of wild-type andmutated proteins were determined by NMR.
Doctoral Research, CERM, University of Florence, Florence, Italy 2001 – 2004
Title: Insights on the cellular function of copper proteins through NMR structural studies Bioinorganic Chemistry
Summary:The research was focused upon the investigation of the structure-function relationship in metalloproteins. This important aspect of structural biology was undertaken by NMR structural and dynamic characterization. In particular the attention was devoted to the processes involved in copper homeostasis, such as copper transfer through the cell membrane, copper transport and delivery within the cell
Laurea in Chemistry, CERM, University of Florence, Florence, Italy 2000
Title: Relation between mobility and function of copper Chaperones
Summary:The dynamic properties of the complex between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase have been studied through NMR spectroscopy. These studies provided insights in the understanding of factors controlling copper transfer.
RESEARCH INTERESTS
The research expertise of Francesca Cantini is focused on structural biology, in particular on the study of structural and dynamic characterization of proteins through NMR spectroscopy. She has contributed to methodological and theoretical advancements in protein characterization by NMR. Since 2000, her research activity is dedicated to the comprehension of processes of copper transport in the cell and its incorporation into the final targets. She is focusing on proteins involved in pathways responsible of copper homeostasis. F.C. is an expert in the characterization of the human Cu, Zn superoxide dismutase protein (hSOD1) and its mutants linked with the amyotrophic lateral sclerosis (ALS). She has structurally characterized, via NMR, different metalleted forms of hSOD1, i.e. zinc-bound hSOD1 with oxidized and reduced disulfide bond and metal-free hSOD1 form with oxidized disulfide bond. These studies were important to understanding the aggregation process of hSOD1 in its metal-free form. F.C is also involved in a collaboration aiming to find leading compounds for the rational design of drug for ALS pathogenesis. During this study the anti-cancer drug cisplatin was found to bind in vitro the hSOD1 enzyme, preventing the protein from aggregating and dissolving existing oligomers. She is also interested in the study of protein folding by in cell NMR. This technique has been applied to characterize the maturation steps of hSOD1 within cell environment.
Among the most important national grants, she was the local coordinator of a granted project (PRIN2012) coordinated by Dr. Orabona (University of Perugia). Within this project F.C. was responsible for carry out NMR ligand-based screening on signal-favoring conformation of the human protein named IDO identifying the most potent ligand binders to the enzyme.
PATENTS
Title: MODIFIED MENINGOCOCCAL FHBP POLYPEPTIDES
Date of Publication: May 2011
AWARDS
“Gastone de Santis” 2010
Division of Chemistry of Biological Systems of the Italian Chemical Society and Italfarmaco Inc.
GRANTS: PRIN2012 Linea d’intervento B Local coordinator of the project 2012S47X27_003 “Approcci integrati per lo studio delle conformazioni di IDO nei disordini immunitari”
PUBLICATIONS
F.C. has co-authored of 49 articles in international scientific journals (with over 1100 citations, h-index = 28) and one book chapter. She has submitted more than 30 NMR structures on PDB.
Several publications are the result of productive collaborations with scientists from prestigious international research centers: Prof. T.V. O’ Halloran (Northwestern University, Evanston, Illinois, USA), Prof. J.S. Valentine (University of California, Los Angeles, USA), Prof. Nigel J. Robinson (University of Newcastle, Newcastle, UK), the nobel prize for chemistry Prof. Kurt Wüthrich (ETH, Zurigo, Svizzera) and Dr. Rino Rappuoli (Global Head of Vaccines Research at Novartis Vaccines and Diagnostics).
Legenda
2007- Current - Permanent Research Scientist at the University of Florence
2001 – 2004 International Ph.D. in Structural Biology, CERM, University of Florence
2000 Laurea in Chemistry, University of Florence, (Graduated Cum Laude 110/110)
The research expertise of Francesca Cantini is focused on structural biology, in particular she focus on the study of structural and dynamic characterization of proteins through NMR spectroscopy. She has contributed to methodological and theoretical advancements in protein characterization by NMR. Since 2000, her research activity is dedicated to the comprehension of processes of metal transport in the cell and its incorporation into the final targets. F.C. is an expert in the characterization of the human Cu, Zn superoxide dismutase protein (hSOD1) and its mutants linked with the amyotrophic lateral sclerosis (ALS). She has structurally characterized, via NMR, different metalleted forms of hSOD1. These studies were important to understanding the aggregation process of hSOD1 in its metal-free form. F.C is also involved in a collaboration aiming to find leading compounds for the rational design of drug for ALS pathogenesis. Recently the anti-cancer drug cisplatin was found to bind in vitro the hSOD1 enzyme, preventing the protein from aggregating and dissolving existing oligomers. She is also interested in the study of protein folding by in cell NMR. This technique has been applied to characterize the maturation steps of hSOD1 within cell environment. F.C. also collaborates with Novartis Vaccines (Siena, Italy) contributing to an innovative approach for the design of new vaccines against pathogens responsible for severe human pathologies for which a preventative therapy is not yet available, i.e. Structural Vaccinology. In this frame she structural characterized proteins considered potential vaccine candidates and she studied their interaction with antibodies. The results obtained from these studies have been used for engineering a chimeric molecule that elicits a broad protective immunity against Neisseria meningitides serogroup B.
