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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

Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.
MA Wright, FA Aprile, P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles
– Chemical Communications
(2015)
51,
14425
Sizing and interactions of proteins under native conditions from microfluidic diffusion measurements: application to molecular chaperones and single-step immunoassay
P Arosio, T Mueller, L Rajah, F Aprile, T Scheidt, J Carrozza, M Wright, M Vendruscolo, C Dobson, T Knowles
– PROTEIN SCIENCE
(2015)
24,
3
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
(2014)
427,
982
Characterization of the conformational fluctuations in the Josephin domain of ataxin-3.
D Sanfelice, A De Simone, A Cavalli, S Faggiano, M Vendruscolo, A Pastore
– Biophys J
(2014)
107,
2923
The H50Q Mutation Induces a 10-fold Decrease in the Solubility of α-Synuclein
R Porcari, C Proukakis, CA Waudby, B Bolognesi, PP Mangione, JFS Paton, S Mullin, LD Cabrita, A Penco, A Relini, G Verona, M Vendruscolo, M Stoppini, GG Tartaglia, C Camilloni, J Christodoulou, AHV Schapira, V Bellotti
– The Journal of biological chemistry
(2014)
290,
2395
ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load
JE Chambers, K Petrova, G Tomba, M Vendruscolo, D Ron
– The Journal of cell biology
(2014)
207,
569
A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein
JR Allison, RC Rivers, JC Christodoulou, M Vendruscolo, CM Dobson
– Biochemistry
(2014)
53,
7170
The CamSol method of rational design of protein mutants with enhanced solubility.
P Sormanni, FA Aprile, M Vendruscolo
– J Mol Biol
(2014)
427,
478
Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein
S Gianni, C Camilloni, R Giri, A Toto, D Bonetti, A Morrone, P Sormanni, M Brunori, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2014)
111,
14141
Identification and characterization of PKCγ, a kinase associated with SCA14, as an amyloidogenic protein
H Takahashi, N Adachi, T Shirafuji, S Danno, T Ueyama, M Vendruscolo, AN Shuvaev, T Sugimoto, T Seki, D Hamada, K Irie, H Hirai, N Sakai, N Saito
– Hum Mol Genet
(2014)
24,
525
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk