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Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

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

Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation
P Flagmeier, G Meisl, M Vendruscolo, TPJ Knowles, CM Dobson, AK Buell, C Galvagnion
– Proc Natl Acad Sci U S A
(2016)
113,
10328
(doi: 10.1073/pnas.1604645113)
Metadynamic metainference: Enhanced sampling of the metainference ensemble using metadynamics
M Bonomi, C Camilloni, M Vendruscolo
– Sci Rep
(2016)
6,
31232
(doi: 10.1038/srep31232)
A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease
R Freer, P Sormanni, G Vecchi, P Ciryam, CM Dobson, M Vendruscolo
– Science Advances
(2016)
2,
e1600947
(doi: 10.1126/sciadv.1600947)
Towards a structural biology of the hydrophobic effect in protein folding.
C Camilloni, D Bonetti, A Morrone, R Giri, CM Dobson, M Brunori, S Gianni, M Vendruscolo
– Scientific Reports
(2016)
6,
28285
(doi: 10.1038/srep28285)
Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein.
C Galvagnion, JWP Brown, MM Ouberai, P Flagmeier, M Vendruscolo, AK Buell, E Sparr, CM Dobson
– Proceedings of the National Academy of Sciences of the United States of America
(2016)
113,
7065
(doi: 10.1073/pnas.1601899113)
Structure of a low-population binding intermediate in protein-RNA recognition
AN Borkar, MF Bardaro, C Camilloni, FA Aprile, G Varani, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2016)
113,
7171
(doi: 10.1073/pnas.1521349113)
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
– Sci Rep
(2016)
6,
27125
(doi: 10.1038/srep27125)
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,
175
(doi: 10.1515/ijnsns-2015-0056)
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,
3116
(doi: 10.1021/acs.biochem.6b00149)
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,
25559
(doi: 10.1038/srep25559)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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