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Centre for Misfolding Diseases

Professor of Biophysics

Our research

In the last 15 years our research has been focused on the development of methods of characterising the structure, dynamics and interactions of proteins in previously inaccessible states. These methods are based on the use of experimental data, in particular from nuclear magnetic resonance spectroscopy, as structural restraints in molecular dynamics simulations. Through this approach it is possible to obtain information about a variety of protein conformations, as for example those populated during the folding process, and about protein interactions in complex environments, including those generating aggregate species that are associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases.

Application to neurodegenerative diseases

More recently, these studies have led us to investigate the physico-chemical principles of proteins homeostasis and their application to the development of therapeutic strategies against neurodegenerative diseases. Starting from the observation that proteins are expressed in the cell at levels close to their solubility limits, we are developing approaches to prevent or delay misfolding disorders based on the enhancement of our quality control mechanisms against protein aggregation.

Watch Professor Vendruscolo discuss his research

Take a tour of the Una Finlay Laboratory in the Centre for Misfolding Diseases

Publications

Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates
S Chia, Z Faidon Brotzakis, RI Horne, A Possenti, B Mannini, R Cataldi, M Nowinska, R Staats, S Linse, TPJ Knowles, J Habchi, M Vendruscolo
– Molecular Pharmaceutics
(2022)
Fragment-based computational design of antibodies targeting structured epitopes
M Aguilar Rangel, A Bedwell, E Costanzi, RJ Taylor, R Russo, GJL Bernardes, S Ricagno, J Frydman, M Vendruscolo, P Sormanni
– Sci Adv
(2022)
8,
eabp9540
Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates
A Horvath, M Vendruscolo, M Fuxreiter
– Biochemistry
(2022)
61,
2461
Protein condensation diseases: therapeutic opportunities
M Vendruscolo, M Fuxreiter
– Nature communications
(2022)
13,
5550
Small soluble α-synuclein aggregates are the toxic species in Parkinson’s disease
D Emin, YP Zhang, E Lobanova, A Miller, X Li, Z Xia, H Dakin, DI Sideris, JYL Lam, RT Ranasinghe, A Kouli, Y Zhao, S De, TPJ Knowles, M Vendruscolo, FS Ruggeri, FI Aigbirhio, CH Williams-Gray, D Klenerman
– Nature Communications
(2022)
13,
5512
Small soluble a-synuclein aggregates are the toxic species in Parkinson’s disease
D Emin, YP Zhang, E Lobanova, A Miller, X Li, Z Xia, H Dakin, DI Sideris, JYL Lam, RT Ranasinghe, A Kouli, Y Zhao, S De, TPJ Knowles, M Vendruscolo, FS Ruggeri, FI Aigbirhio, CH Williams-Gray, D Klenerman
– Nat Commun
(2022)
13,
5512
Effects of N-terminal Acetylation on the Aggregation of Disease-related α-synuclein Variants: N-terminal acetylation of α-synuclein variants
R Bell, M Castellana-Cruz, A Nene, RJ Thrush, CK Xu, JR Kumita, M Vendruscolo
– Journal of molecular biology
(2022)
167825
Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species.
G Fani, CE La Torre, R Cascella, C Cecchi, M Vendruscolo, F Chiti
– Cellular and Molecular Life Sciences
(2022)
79,
500
The N-terminal acetylation of α-synuclein slows down its aggregation process and alters the morphology of the resulting aggregates
R Bell, RJ Thrush, M Castellana-Cruz, M Oeller, R Staats, A Nene, P Flagmeier, CK Xu, S Satapathy, C Galvagnion, MR Wilson, CM Dobson, JR Kumita, M Vendruscolo
– Biochemistry
(2022)
61,
1743
ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy
C Olivieri, GC Li, Y Wang, M V S, C Walker, J Kim, C Camilloni, A De Simone, M Vendruscolo, DA Bernlohr, SS Taylor, G Veglia
– Sci Adv
(2022)
8,
eabo0696
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Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address