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

Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism
C Camilloni, AB Sahakyan, MJ Holliday, NG Isern, F Zhang, EZ Eisenmesser, M Vendruscolo
Proc Natl Acad Sci U S A
(2014)
111
Statistical Mechanics of the Denatured State of a Protein Using Replica-Averaged Metadynamics
C Camilloni, M Vendruscolo
Journal of the American Chemical Society
(2014)
136
A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings
C Camilloni, M Vendruscolo
J Phys Chem B
(2014)
119
ALMOST: An all atom molecular simulation toolkit for protein structure determination
B Fu, AB Sahakyan, C Camilloni, GG Tartaglia, E Paci, A Caflisch, M Vendruscolo, A Cavalli
Journal of Computational Chemistry
(2014)
35
Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour
G Fusco, A De Simone, T Gopinath, V Vostrikov, M Vendruscolo, CM Dobson, G Veglia
Nat Commun
(2014)
5
The amyloid state and its association with protein misfolding diseases
TPJ Knowles, M Vendruscolo, CM Dobson
Nature reviews. Molecular cell biology
(2014)
15
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation
AK Buell, C Galvagnion, R Gaspar, E Sparr, M Vendruscolo, TPJ Knowles, S Linse, CM Dobson
Proceedings of the National Academy of Sciences
(2014)
111
Understanding the influence of codon translation rates on cotranslational protein folding.
EP O'Brien, P Ciryam, M Vendruscolo, CM Dobson
Accounts of Chemical Research
(2014)
47
New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics
R Montalvao, C Camilloni, A De Simone, M Vendruscolo
Journal of Biomolecular NMR
(2014)
58
Structural investigation of the folding of an immunoglobulin domain on the ribosome using NMR Spectroscopy
A Cassaignau, L Cabrita, C Waudby, X Wang, H Launay, C Camilloni, M-E Karyadi, S Chan, M Vendruscolo, C Dobson, J Christodoulou
FASEB JOURNAL
(2014)
28

Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address