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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

Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.
M Zhu, A De Simone, D Schenk, G Toth, CM Dobson, M Vendruscolo
– The Journal of chemical physics
(2013)
139,
035101-1
(doi: 10.1063/1.4811831)
A geometrical parametrization of C1'-C5' RNA ribose chemical shifts calculated by density functional theory.
R Suardíaz, AB Sahakyan, M Vendruscolo
– The Journal of Chemical Physics
(2013)
139,
034101
(doi: 10.1063/1.4811498)
Single-molecule measurements of transient biomolecular complexes through microfluidic dilution.
MH Horrocks, L Rajah, P Jönsson, M Kjaergaard, M Vendruscolo, TPJ Knowles, D Klenerman
– Anal Chem
(2013)
85,
6855
(doi: 10.1021/ac4010875)
A method of determining RNA conformational ensembles using structure-based calculations of residual dipolar couplings
AN Borkar, A De Simone, RW Montalvao, M Vendruscolo
– J Chem Phys
(2013)
138,
215103
(doi: 10.1063/1.4804301)
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
SIA Cohen, S Linse, LM Luheshi, E Hellstrand, DA White, L Rajah, DE Otzen, M Vendruscolo, CM Dobson, TPJ Knowles
– Proceedings of the National Academy of Sciences
(2013)
110,
9758
(doi: 10.1073/pnas.1218402110)
Integration and characterization of solid wall electrodes in microfluidic devices fabricated in a single photolithography step
TW Herling, T Müller, L Rajah, JN Skepper, M Vendruscolo, TPJ Knowles
(2013)
(doi: 10.48550/arxiv.1305.3554)
Integration and characterization of solid wall electrodes in microfluidic devices fabricated in a single photolithography step
TW Herling, T Müller, L Rajah, JN Skepper, M Vendruscolo, TPJ Knowles
– Applied Physics Letters
(2013)
102,
184102
(doi: 10.1063/1.4803917)
The codon information index: A quantitative measure of the information provided by the codon bias
L Caniparoli, M Marsili, M Vendruscolo
– Journal of Statistical Mechanics Theory and Experiment
(2013)
2013,
P04031
(doi: 10.1088/1742-5468/2013/04/P04031)
Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics
D Granata, C Camilloni, M Vendruscolo, A Laio
– Proceedings of the National Academy of Sciences of the United States of America
(2013)
110,
6817
(doi: 10.1073/pnas.1218350110)
Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages.
T Guilliams, F El-Turk, AK Buell, EM O'Day, FA Aprile, EK Esbjörner, M Vendruscolo, N Cremades, E Pardon, L Wyns, ME Welland, J Steyaert, J Christodoulou, CM Dobson, E De Genst
– Journal of molecular biology
(2013)
425,
2397
(doi: 10.1016/j.jmb.2013.01.040)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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