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

Metastability of native proteins and the phenomenon of amyloid formation
AJ Baldwin, TPJ Knowles, GG Tartaglia, AW Fitzpatrick, GL Devlin, SL Shammas, CA Waudby, MF Mossuto, S Meehan, SL Gras, J Christodoulou, SJ Anthony-Cahill, PD Barker, M Vendruscolo, CM Dobson
J Am Chem Soc
(2011)
133
Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations.
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
The Journal of Chemical Physics
(2011)
135
Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments.
SIA Cohen, M Vendruscolo, ME Welland, CM Dobson, EM Terentjev, TPJ Knowles
The Journal of chemical physics
(2011)
135
Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations.
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
The Journal of Chemical Physics
(2011)
135
The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein.
L Kang, K-P Wu, M Vendruscolo, J Baum
J Am Chem Soc
(2011)
133
Protein solubility and protein homeostasis: a generic view of protein misfolding disorders.
M Vendruscolo, TPJ Knowles, CM Dobson
Cold Spring Harbor Perspectives in Biology
(2011)
3
Structure-based prediction of methyl chemical shifts in proteins
AB Sahakyan, WF Vranken, A Cavalli, M Vendruscolo
Journal of Biomolecular NMR
(2011)
50
Kinetics of protein aggregation
T Knowles, M Vendruscolo, C Dobson
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2011)
40
Structure-based prediction of methyl chemical shifts in proteins.
AB Sahakyan, WF Vranken, A Cavalli, M Vendruscolo
J Biomol NMR
(2011)
50
Excited-state control of protein activity.
M Vendruscolo
Journal of molecular biology
(2011)
412

Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address