skip to content

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

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
Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.
P Ciryam, R Kundra, RI Morimoto, CM Dobson, M Vendruscolo
– Trends in Pharmacological Sciences
(2015)
36,
72
Analysis of the hierarchical structure of the B. subtilis transcriptional regulatory network.
S Kumar, M Vendruscolo, A Singh, D Kumar, A Samal
– Mol Biosyst
(2015)
11,
930
Structure of a low-population intermediate state in the release of an enzyme product.
A De Simone, FA Aprile, A Dhulesia, CM Dobson, M Vendruscolo
– Elife
(2015)
2015,
e02777
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
Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases
P Ciryam, R Kundra, RI Morimoto, CM Dobson, M Vendruscolo
– Trends in Pharmacological Sciences
(2015)
36,
72
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
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
C Galvagnion, AK Buell, G Meisl, TC Michaels, M Vendruscolo, TPJ Knowles, CM Dobson
– EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44,
S101
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
– Chem Commun (Camb)
(2015)
51,
14425
Rapid sizing of proteins in complex solutions
P Arosio, T Muller, L Rajah, EV Yates, FA Aprile, SIA Cohen, DA White, TW Herling, E de Genst, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles
– EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2015)
44,
S49
  • <
  • 45 of 80
  • >

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk