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Centre for Misfolding Diseases

Giuliana Fusco

I am a research fellow of the St John's College studying the molecular properties of alpha-synuclein, the central protein for Parkinson's disease, under functional and pathological conditions. We combine biomolecular NMR spectroscopy in solution-state and in solid-state as well as cryo-EM, super-resolution microscopy, single molecule FRET and cellular biophysics to obtain accurate characterisation of transient interactions established by alpha-synuclein with various cellular components. A key interest is in the membrane interactions, which are crucial for this protein to drive the biological behaviour of both its functional monomeric state and the disease-associated aggregates.

Selected Publications

Fusco G, Chen SW, Williamson PT, Cascella R, Perni M, Jarvis JA, Cecchi C, Vendruscolo M, Chiti F, Cremades N, Ying L, Dobson CM, De Simone A “Structural Basis of Membrane Disruption and Cellular Toxicity by α-Synuclein Oligomers” Science, 2017, 358:1440-3

Fusco G, Pape T, Mahou P, Costa AR, Kaminski CF, Kaminski Schierle G, Vendruscolo M, Veglia G, Dobson CM, De Simone A “Structural basis of synaptic vesicle assembly induced by α-synuclein”. Nature Communications, 2016, 7:12563 

Fusco G, De Simone A, Gopinath T, Vostikov V, Vendruscolo M,  Dobson CM, Veglia G. “Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour ”. Nature Communications, 2014,5:3827.

Man WK, De TahirbegiB, Vrettas M, Preet S, Ying L, Vendruscolo M, De Simone A*, Fusco G* “The Docking of Synaptic Vesicles on the Presynaptic Membrane Induced by α Synuclein is Modulated by Lipid Composition” Nature Communications, 2021, 12(1):927

Runfola M, De Simone A, Vendruscolo M, Dobson CM, Fusco G* “The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State” Scientific Reports, 2020, 10:204

Postdoctoral researcher

Telephone number

01223 763842

Email address