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

New scenarios of protein folding can occur on the ribosome
EP O'Brien, J Christodoulou, M Vendruscolo, CM Dobson
Journal of the American Chemical Society
(2011)
133
On the Effect of the Ribosome and Trigger Factor on Nascent Chain Protein Folding
EP O'Brien, J Christodoulou, C Dobson, M Vendruscolo
BIOPHYSICAL JOURNAL
(2011)
100
Focus on physical principles of protein behavior in the cell.
M Porto, HE Roman, M Vendruscolo
Proteomics
(2010)
10
Interactions in the native state of monellin, which play a protective role against aggregation.
O Szczepankiewicz, C Cabaleiro-Lago, GG Tartaglia, M Vendruscolo, T Hunter, GJ Hunter, H Nilsson, E Thulin, S Linse
Molecular bioSystems
(2010)
7
Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain.
S Gianni, Y Ivarsson, A De Simone, C Travaglini-Allocatelli, M Brunori, M Vendruscolo
Nature Structural & Molecular Biology
(2010)
17
Transient tertiary structure formation within the ribosome exit port
EP O'Brien, S-TD Hsu, J Christodoulou, M Vendruscolo, CM Dobson
J Am Chem Soc
(2010)
132
Translationally optimal codons associate with aggregation-prone sites in proteins
Y Lee, T Zhou, GG Tartaglia, M Vendruscolo, CO Wilke
Proteomics
(2010)
10
Derivation of a solubility condition for proteins from an analysis of the competition between folding and aggregation
S Pechmann, M Vendruscolo
Mol Biosyst
(2010)
6
Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR
MA Caporini, VS Bajaj, M Veshtort, A Fitzpatrick, CE MacPhee, M Vendruscolo, CM Dobson, RG Griffin
Journal of Physical Chemistry B
(2010)
114
Enzymatic activity in disordered states of proteins.
M Vendruscolo
Curr Opin Chem Biol
(2010)
14

Research Interest Groups

Telephone number

01223 763873

Email address