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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

Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity.
– PLoS biology
(2007)
5,
Systematic in vivo analysis of the intrinsic determinants of amyloid beta pathogenicity
LM Luheshi, GG Tartaglia, A-C Brorsson, AP Pawar, IE Watson, F Chiti, M Vendruscolo, DA Lomas, CM Dobson, DC Crowther
– PLoS biology
(2007)
5,
e290
Importance of metastable states in the free energy landscapes of polypeptide chains.
S Auer, MA Miller, SV Krivov, CM Dobson, M Karplus, M Vendruscolo
– Phys Rev Lett
(2007)
99,
178104
More charges against aggregation
M Vendruscolo, CM Dobson
– Nature
(2007)
449,
555
Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.
M Cheon, I Chang, S Mohanty, LM Luheshi, CM Dobson, M Vendruscolo, G Favrin
– PLoS Computational Biology
(2007)
3,
1727
The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution
E Monsellier, M Ramazzotti, PP de Laureto, G-G Tartaglia, N Taddei, A Fontana, M Vendruscolo, F Chiti
– Biophysical journal
(2007)
93,
4382
COMP 492-Caught in atomistic detailed action: Modeling of protein-G monomers forming oligomers
JM Bui, J Gsponer, JC Wooley, M Vendruscolo, JA McCammon, CM Dobson
– ABSTR PAP AM CHEM S
(2007)
234,
Characterization of the nucleation barriers for protein aggregation and amyloid formation.
S Auer, CM Dobson, M Vendruscolo
– All Life
(2007)
1,
137
Magnetic-Phase Transitions of Ising Surfaces with Modified Surface-Bulk Coupling: a Monte Carlo Study
M VENDRUSCOLO, M ROVERE, A FASOLINO
– EPL (Europhysics Letters)
(2007)
20,
547
Molecular dynamics simulations from putative transition states of alpha-spectrin SH3 domain.
X Periole, M Vendruscolo, AE Mark
– Proteins
(2007)
69,
536
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk