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Yusuf Hamied Department of Chemistry

 

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

β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces
JWP Brown, AK Buell, TCT Michaels, G Meisl, J Carozza, P Flagmeier, M Vendruscolo, TPJ Knowles, CM Dobson, C Galvagnion
– Scientific reports
(2016)
6,
36010
Structural basis of synaptic vesicle assembly promoted by α-synuclein
G Fusco, T Pape, AD Stephens, P Mahou, AR Costa, CF Kaminski, GS Kaminski Schierle, M Vendruscolo, G Veglia, CM Dobson, A De Simone
– Nature communications
(2016)
7,
12563
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
– Proceedings of the National Academy of Sciences of the United States of America
(2016)
113,
10328
Metadynamic metainference: Enhanced sampling of the metainference ensemble using metadynamics.
M Bonomi, C Camilloni, M Vendruscolo
– Scientific reports
(2016)
6,
31232
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
– Sci Adv
(2016)
2,
e1600947
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
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
– Proc Natl Acad Sci U S A
(2016)
113,
7065
Structure of a low-population binding intermediate in protein-RNA recognition.
AN Borkar, MF Bardaro, C Camilloni, FA Aprile, G Varani, M Vendruscolo
– Proc Natl Acad Sci U S A
(2016)
113,
7171
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,
27125
Particle-Based Monte-Carlo Simulations of Steady-State Mass Transport at Intermediate Péclet 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
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk