Fino ad Aprile 2026 sono disponibili due tutor per l'esame di chimica: Giacomo Venditti E-mail: giacomo.venditti@edu.unifi.it Tel: 320 5340913 Francesco Luigi Lopez E-mail: francesco.lopez@edu.unifi.it Tel: +39 334 2438157
Fabrizio Chiti si è laureato in Scienze Biologiche nel 1995 all'Univeristà di Firenze ed ha conseguito il dottorato di ricerca in Chimica presso l'Università di Oxford (UK) nel 1999. La sua attività di ricerca, svolta sotto la supervisione del Prof. C.M. Dobson, ha riguardato in questo periodo il folding proteico. La sua attività di ricerca post-dottorato, svolta nel campo dell'aggregazione proteica e della formazione di fibrille amiloidi, è stata condotta all'Università di Firenze per due anni, sotto la guida del Prof. G. Ramponi, e quindi all'Università di Cambridge per 1 anno, ancora sotto la guida del Prof. C.M. Dobson.
Fabrizio Chiti è stato quindi Professore Associato di Biochimica dal 2002 al 2010 ed è adesso Professore Ordinario presso il Dipartimento di Scienze Biomediche Sperimentali e Cliniche, Sezione di Scienze Biochimiche, dell'Università di Firenze.
Personalia
Education
Research Experience
Academic Honours
Recent Lectures at International Meetings (years 2002-2013)
Teaching
Invited Reviews and Book Chapters
Publications of original articles (excluding reviews)
Proteins have a generic tendency to convert from their soluble states into insoluble highly structured aggregates known as amyloid fibrils. Since these aggregates are toxic to the cells, especially in the form of early forming oligomers, the cellular machinery has evolved, among other requirements, to inhibit uncontrolled protein aggregation. Failure to inhibit protein aggregation often results in pathology. To date, a large number of very diverse human diseases, including Alzheimer's, Parkinson's disease and type II diabetes, have been recognised to be associated with the formation of amyloid fibrils or protein inclusions with amyloid-like properties. Amyloid fibril formation is also exploited by living organisms for the formation of fibrillar structures with specific biological functions, provided that this occurs under controlled conditions. Finally, the recent findings that the inclusion bodies formed after overexpression of heterologous proteins in bacteria are amyloid-like in structure and the increasing awareness that an enormous number of novel materials based on the amyloid motif can be constructed has expanded the interest of amyloid formation to biotechnology.
Legenda
Fabrizio Chiti received his Degree in Biological Science in 1995 at the University of Florence in Italy and his PhD in Chemistry in 1999 at the University of Oxford. His research, performed under the supervision of Prof. C.M. Dobson, concerned protein folding studies. His post-doctoral work, performed in the field of protein aggregation and amyloid formation, was carried out at the University of Florence for 2 years and at the University of Cambridge for 1 year.
He was then appointed Associate Professor of Biochemistry from 2002 to 2010 and is now Full Professor at the Department of Biomedical Experimental and Clicial Sciences, Section of Biochemistry, of the University of Florence.
