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

Structural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity.
G Fusco, A De Simone, P Arosio, M Vendruscolo, G Veglia, CM Dobson
Scientific reports
(2016)
6
Particle-Based Monte-Carlo Simulations of Steady-State Mass Transport at Intermediate Peclet Numbers
T Müller, P Arosio, L Rajah, SIA Cohen, EV Yates, M Vendruscolo, CM Dobson, TPJ Knowles
International Journal of Nonlinear Sciences and Numerical Simulation
(2016)
17
Structural Effects of Two Camelid Nanobodies Directed to Distinct C-Terminal Epitopes on α-Synuclein
F El-Turk, FN Newby, E De Genst, T Guilliams, T Sprules, A Mittermaier, CM Dobson, M Vendruscolo
Biochemistry
(2016)
55
Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability
C Camilloni, BM Sala, P Sormanni, R Porcari, A Corazza, M De Rosa, S Zanini, A Barbiroli, G Esposito, M Bolognesi, V Bellotti, M Vendruscolo, S Ricagno
Scientific reports
(2016)
6
Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor
A Deckert, CA Waudby, T Wlodarski, AS Wentink, X Wang, JP Kirkpatrick, JFS Paton, C Camilloni, P Kukic, CM Dobson, M Vendruscolo, LD Cabrita, J Christodoulou
Proceedings of the National Academy of Sciences
(2016)
113
A transcriptional signature of Alzheimer’s disease is associated with a metastable subproteome at risk for aggregation
P Ciryam, R Kundra, R Freer, RI Morimoto, CM Dobson, M Vendruscolo
Proceedings of the National Academy of Sciences
(2016)
113
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.
P Arosio, TCT Michaels, S Linse, C Månsson, C Emanuelsson, J Presto, J Johansson, M Vendruscolo, CM Dobson, TPJ Knowles
Nat Commun
(2016)
7
Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain
D Bonetti, C Camilloni, L Visconti, S Longhi, M Brunori, M Vendruscolo, S Gianni
Journal of Biological Chemistry
(2016)
291
A structural ensemble of a ribosome–nascent chain complex during cotranslational protein folding
LD Cabrita, AME Cassaignau, HMM Launay, CA Waudby, T Wlodarski, C Camilloni, M-E Karyadi, AL Robertson, X Wang, AS Wentink, L Goodsell, CA Woolhead, M Vendruscolo, CM Dobson, J Christodoulou
Nature structural & molecular biology
(2016)
23
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.
P Joshi, S Chia, J Habchi, TPJ Knowles, CM Dobson, M Vendruscolo
ACS Comb Sci
(2016)
18

Co-Director

Research Interest Groups

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01223 763873

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