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

Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements.

JR Allison, P Varnai, CM Dobson, M Vendruscolo

J Am Chem Soc

(2009)

131

18314

(doi: 10.1021/ja904716h)

Analysis of Sub-τ_c and Supra-τ_c Motions in Protein Gβ1 Using Molecular Dynamics Simulations

JM Bui, J Gsponer, M Vendruscolo, CM Dobson

Biophysical Journal

(2009)

97

2513

(doi: 10.1016/j.bpj.2009.07.061)

Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins.

A De Simone, A Cavalli, S-TD Hsu, W Vranken, M Vendruscolo

J Am Chem Soc

(2009)

131

16332

(doi: 10.1021/ja904937a)

Quantitative approaches to defining normal and aberrant protein homeostasis.

M Vendruscolo, CM Dobson

Faraday discussions

(2009)

143

277

(doi: 10.1039/b905825g)

Fast and Accurate Predictions of Protein NMR Chemical Shifts from Interatomic Distances

KJ Kohlhoff, P Robustelli, A Cavalli, X Salvatella, M Vendruscolo

Journal of the American Chemical Society

(2009)

131

13894

(doi: 10.1021/ja903772t)

Correlation between mRNA expression levels and protein aggregation propensities in subcellular localisations

GG Tartaglia, M Vendruscolo

Mol Biosyst

(2009)

5

1873

(doi: 10.1039/b913099n)

Prediction of folding and misfolding of proteins from their amino acid sequences

M Vendruscolo

ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY

(2009)

238

A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation

S Auer, A Trovato, M Vendruscolo

PLoS computational biology

(2009)

5

e1000458

(doi: 10.1371/journal.pcbi.1000458)

On the mechanism of nonspecific inhibitors of protein aggregation: Dissecting the interactions of α-synuclein with congo red and lacmoid

C Lendel, CW Bertoncini, N Cremades, CA Waudby, M Vendruscolo, CM Dobson, D Schenk, J Christodoulou, G Toth

Biochemistry

(2009)

48

8322

(doi: 10.1021/bi901285x)

Efficient identification of near-native conformations in ab initio protein structure prediction using structural profiles

K Wolff, M Vendruscolo, M Porto

Proteins Structure Function and Bioinformatics

(2009)

78

249

(doi: 10.1002/prot.22533)