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

EGCG inactivates a pore-forming toxin by promoting its oligomerization and decreasing its solvent-exposed hydrophobicity
JM Gabriel, T Tan, DJ Rinauro, CM Hsu, CJ Buettner, M Gilmer, A Kaur, TL McKenzie, M Park, S Cohen, S Errico, AK Wright, F Chiti, M Vendruscolo, R Limbocker
Chemico-Biological Interactions
(2022)
371
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)
20
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
Science Advances
(2022)
8
Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates
A Horvath, M Vendruscolo, M Fuxreiter
Biochemistry
(2022)
61
Multi-dimensional protein solubility optimization with an ultra-high-throughput microfluidic platform
NA Erkamp, M Oeller, T Sneideris, H AusserwÓ§ger, A Levin, T Welsh, R Qi, D Qian, H Zhu, P Sormanni, M Vendruscolo, TPJ Knowles
(2022)
Characterization of full-length p53 aggregates and their kinetics of formation
L Julian, JC Sang, Y Wu, G Meisl, JH Brelstaff, A Miller, MR Cheetham, M Vendruscolo, TPJ Knowles, FS Ruggeri, C Bryant, S Ros, KM Brindle, D Klenerman
Biophys J
(2022)
121
Protein condensation diseases: therapeutic opportunities
M Vendruscolo, M Fuxreiter
Nature Communications
(2022)
13
An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients.
K Kulenkampff, D Emin, R Staats, YP Zhang, L Sakhnini, A Kouli, O Rimon, E Lobanova, CH Williams-Gray, FA Aprile, P Sormanni, D Klenerman, M Vendruscolo
Chem Sci
(2022)
13
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
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

Research Interest Groups

Telephone number

01223 763873

Email address