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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

Structure and dynamics of GeoCyp: A thermophilic cyclophilin with a novel substrate binding mechanism that functions efficiently at low temperatures
MJ Holliday, C Camilloni, GS Armstrong, NG Isern, F Zhang, M Vendruscolo, EZ Eisenmesser
– Biochemistry
(2015)
54,
3207
(doi: 10.1021/acs.biochem.5b00263)
Widespread Proteome Remodeling and Aggregation in Aging C. elegans.
DM Walther, P Kasturi, M Zheng, S Pinkert, G Vecchi, P Ciryam, RI Morimoto, CM Dobson, M Vendruscolo, M Mann, FU Hartl
– Cell
(2015)
161,
919
(doi: 10.1016/j.cell.2015.03.032)
Structure and Dynamics of the Integrin LFA-1 I-Domain in the Inactive State Underlie its Inside-Out/Outside-In Signaling and Allosteric Mechanisms
P Kukic, HT Alvin Leung, F Bemporad, FA Aprile, JR Kumita, A De Simone, C Camilloni, M Vendruscolo
– Structure
(2015)
23,
745
(doi: 10.1016/j.str.2014.12.020)
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
SIA Cohen, P Arosio, J Presto, FR Kurudenkandy, H Biverstål, L Dolfe, C Dunning, X Yang, B Frohm, M Vendruscolo, J Johansson, CM Dobson, A Fisahn, TPJ Knowles, S Linse
– Nature structural & molecular biology
(2015)
22,
207
(doi: 10.1038/nsmb.2971)
The physical basis of protein misfolding disorders
TPJ Knowles, M Vendruscolo, CM Dobson
– Physics Today
(2015)
68,
36
(doi: 10.1063/PT.3.2719)
The s2D method: Simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins
P Sormanni, C Camilloni, P Fariselli, M Vendruscolo
– Journal of Molecular Biology
(2015)
427,
982
(doi: 10.1016/j.jmb.2014.12.007)
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
SIA Cohen, P Arosio, J Presto, FR Kurudenkandy, H Biverstal, L Dolfe, C Dunning, X Yang, B Frohm, M Vendruscolo, J Johansson, CM Dobson, A Fisahn, TPJ Knowles, S Linse
– Nature Structural & Molecular Biology
(2015)
22,
207
(doi: 10.1038/nsmb.2971)
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.
C Galvagnion, AK Buell, G Meisl, TCT Michaels, M Vendruscolo, TPJ Knowles, CM Dobson
– Nature chemical biology
(2015)
11,
229
(doi: 10.1038/NCHEMBIO.1750)
The CamSol method of rational design of protein mutants with enhanced solubility
P Sormanni, FA Aprile, M Vendruscolo
– Journal of Molecular Biology
(2015)
427,
478
(doi: 10.1016/j.jmb.2014.09.026)
Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases
P Ciryam, R Kundra, RI Morimoto, CM Dobson, M Vendruscolo
– Trends Pharmacol Sci
(2015)
36,
72
(doi: 10.1016/j.tips.2014.12.004)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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