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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

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,
278
(doi: 10.1038/nsmb.3182)
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,
144
(doi: 10.1021/acscombsci.5b00129)
Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein
A Toto, C Camilloni, R Giri, M Brunori, M Vendruscolo, S Gianni
– Sci Rep
(2016)
6,
21994
(doi: 10.1038/srep21994)
Neuroscience: An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Ab42 aggregates linked with Alzheimer's disease
J Habchi, P Arosio, M Perni, AR Costa, M Yagi-Utsumi, P Joshi, S Chia, SIA Cohen, MBD Müller, S Linse, EAA Nollen, CM Dobson, TPJ Knowles, M Vendruscolo
– Science advances
(2016)
2,
e1501244
(doi: 10.1126/sciadv.1501244)
Hamiltonian Dynamics of Protein Filament Formation.
TCT Michaels, SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
– Phys Rev Lett
(2016)
116,
038101
(doi: 10.1103/physrevlett.116.038101)
Molecular mechanisms of protein aggregation from global fitting of kinetic models.
G Meisl, JB Kirkegaard, P Arosio, TCT Michaels, M Vendruscolo, CM Dobson, S Linse, TPJ Knowles
– Nature protocols
(2016)
11,
252
(doi: 10.1038/nprot.2016.010)
Metainference: A Bayesian inference method for heterogeneous systems.
M Bonomi, C Camilloni, A Cavalli, M Vendruscolo
– Science Advances
(2016)
2,
e1501177
(doi: 10.1126/sciadv.1501177)
Determination of statistical ensembles of intrinsically disordered proteins using NMR measurements
M Vendruscolo
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2016)
252,
(link to publication)
Characterizing the free energy landscape of intrinsically disordered proteins by metadynamics simulation and experiments
D Granata, G Zerze, J Mittal, M Vendruscolo, A Laio
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2016)
252,
(link to publication)
Structural Insights into the Calcium-Mediated Allosteric Transition in the C-Terminal Domain of Calmodulin from Nuclear Magnetic Resonance Measurements.
P Kukic, P Lundström, C Camilloni, J Evenäs, M Akke, M Vendruscolo
– Biochemistry
(2015)
55,
19
(doi: 10.1021/acs.biochem.5b00961)
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Research Groups

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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