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 acidmutations 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]
↑Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, Evangelisti E, Relini A, Stefani M, Dobson CM, Cecchi C, Chiti F (February 2010). "A causative link between the structure of aberrant protein oligomers and their toxicity". Nature Chemical Biology. 6 (2): 140–7. doi:10.1038/nchembio.283. hdl:2158/382930. PMID20081829. S2CID43311039.
