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

Chemical kinetics for drug discovery to combat protein aggregation diseases
P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles
Trends in Pharmacological Sciences
(2014)
35
Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease
G Tóth, SJ Gardai, W Zago, CW Bertoncini, N Cremades, SL Roy, MA Tambe, J-C Rochet, C Galvagnion, G Skibinski, S Finkbeiner, M Bova, K Regnstrom, S-S Chiou, J Johnston, K Callaway, JP Anderson, MF Jobling, AK Buell, TA Yednock, TPJ Knowles, M Vendruscolo, J Christodoulou, CM Dobson, D Schenk, L McConlogue
PloS one
(2014)
9
The dynamics of interleukin-8 and its interaction with human CXC receptor i peptide
AA Kendrick, MJ Holliday, NG Isern, F Zhang, C Camilloni, C Huynh, M Vendruscolo, G Armstrong, EZ Eisenmesser
Protein Sci
(2014)
23
A conformational ensemble derived using NMR methyl chemical shifts reveals a mechanical clamping transition that gates the binding of the HU protein to dna
A Kannan, C Camilloni, AB Sahakyan, A Cavalli, M Vendruscolo
Journal of the American Chemical Society
(2014)
136
A simple lattice model that captures protein folding, aggregation and amyloid formation
S Abeln, M Vendruscolo, CM Dobson, D Frenkel
PLoS ONE
(2014)
9
Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.
EP O'Brien, M Vendruscolo, CM Dobson
Nat Commun
(2014)
5
Elucidating the Structural Basis of α-Synuclein Fibrillation using Small Camelid Nanobodies
FE Turk, G Tomba, E De Genst, T Guillams, P Kukic, M Vendruscolo, C Dobson
Biophysical Journal
(2014)
106
Determination of Primary Nucleation Mechanisms of α-Synuclein Amyloid Aggregation
FA Aprile, G Meisl, AK Buell, P Flagmeier, CM Dobson, M Vendruscolo, TPJ Knowles
Biophysical Journal
(2014)
106
Conformational Equilibrium between the Sub States of the Acidic Denatured State of ACBP Determined by NMR Chemical Shifts and Metadynamics
C Camilloni, M Vendruscolo
Biophysical Journal
(2014)
106
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