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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

Determination of the Structure and Dynamics of the Fuzzy Coat of an Amyloid Fibril of IAPP Using Cryo-Electron Microscopy
Z Faidon Brotzakis, T Löhr, S Truong, S Hoff, M Bonomi, M Vendruscolo
– Biochemistry
(2023)
62,
2407
Quantitative Attribution of the Protective Effects of Aminosterols against Protein Aggregates to Their Chemical Structures and Ability to Modulate Biological Membranes.
S Errico, G Lucchesi, D Odino, EY Osman, R Cascella, L Neri, C Capitini, M Calamai, F Bemporad, C Cecchi, WA Kinney, D Barbut, A Relini, C Canale, G Caminati, R Limbocker, M Vendruscolo, M Zasloff, F Chiti
– J Med Chem
(2023)
66,
9519
Amyloid formation as a protein phase transition
TCT Michaels, D Qian, A Šarić, M Vendruscolo, S Linse, TPJ Knowles
– Nature Reviews Physics
(2023)
5,
379
Extracellular protein homeostasis: The dawning of a new age for human disease therapies?
MR Wilson, S Satapathy, M Vendruscolo
– Clinical and translational medicine
(2023)
13,
e1305
Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation
M Vendruscolo
– Expert opinion on drug discovery
(2023)
18,
881
Case report of a patient with unclassified tauopathy with molecular and neuropathological features of both progressive supranuclear palsy and corticobasal degeneration.
S Koga, MA Metrick, LI Golbe, A Santambrogio, M Kim, AI Soto-Beasley, RL Walton, MC Baker, CF De Castro, M DeTure, D Russell, BA Navia, C Sandiego, OA Ross, M Vendruscolo, B Caughey, DW Dickson
– Acta Neuropathologica Communications
(2023)
11,
88
CAID prediction portal: a comprehensive service for predicting intrinsic disorder and binding regions in proteins.
A Del Conte, A Bouhraoua, M Mehdiabadi, D Clementel, AM Monzon, CAID predictors, SCE Tosatto, D Piovesan
– Nucleic Acids Research
(2023)
51,
W62
α-Synuclein oligomers form by secondary nucleation
C Xu, G Meisl, E Andrzejewska, G Krainer, A Dear, MC Cruz, S Turi, R Jacquat, W Arter, M Vendruscolo, S Linse, TPJ Knowles
(2023)
Towards sequence-based principles for protein phase separation predictions.
M Vendruscolo, M Fuxreiter
– Current opinion in chemical biology
(2023)
75,
102317
Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains
A Miller, J Wei, S Meehan, CM Dobson, ME Welland, D Klenerman, M Vendruscolo, FS Ruggeri, TPJ Knowles
– Proc Natl Acad Sci U S A
(2023)
120,
e2216234120
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Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address