| Fabrizio Chiti | |
| Birth Date: | 1971 7, df=y |
| Birth Place: | Florence, Italy |
| Fields: | Biophysics, Biochemistry |
| Workplaces: | Department of Experimental and Clinical Biomedical Sciences, University of Florence |
| Alma Mater: | Biological Sciences, University of Florence, Italy(E.N.S., 1995) |
| Doctoral Advisor: | Chris Dobson |
| Academic Advisors: | Giampietro Ramponi, Chris Dobson |
| Known For: | Protein aggregation and amyloid |
Fabrizio Chiti (born in Florence, 7 July 1971) is an Italian biochemist noted for his work on Protein aggregation and amyloid.[1]
Chiti is a graduate in Biological Sciences of the University of Florence (Italy).[2] He attained a PhD degree (D.Phil) in Chemistry in 2000 at the University of Oxford in UK.[2] He then worked as a postdoctoral researcher at the University of Florence, Italy, with Giampietro Ramponi as a supervisor (2000–2002) and at the University of Cambridge, UK, under the supervision of Chris Dobson (2002).[2]
He was appointed as an Associate (2002) and then Full Professor (2010) at the University of Florence in Biochemistry.[2] Chiti provided contributions in the field of misfolding and aggregation, particularly in the field of amyloid[1] He rationalized how amino acid mutations induce protein aggregation and edited an equation to predict the effect of mutations on the aggregation of an unfolded protein,[3] [4] which led to a search by many investigators of algorithms with predictive power on essential aspects of protein aggregation. He also correlated the toxicities of abnormal protein oligomers with specific structural properties of them.[5] His 2006 review with Chris Dobson on protein misfolding, amyloid formation and human disease,[6] later updated as a new report,[7] is a reference paper in the field of amyloid and received, as of October 2019, more than four thousands citations in scientific publications.[1] [8]