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

Folding of small proteins by Monte Carlo simulations with chemical shift restraints without the use of molecular fragment replacement or structural homology.

P Robustelli, A Cavalli, CM Dobson, M Vendruscolo, X Salvatella

The journal of physical chemistry. B

(2009)

113

7890

(doi: 10.1021/jp900780b)

A relationship between mRNA expression levels and protein solubility in E. coli.

GG Tartaglia, S Pechmann, CM Dobson, M Vendruscolo

J Mol Biol

(2009)

388

381

(doi: 10.1016/j.jmb.2009.03.002)

Toward an accurate determination of free energy landscapes in solution states of proteins

A De Simone, B Richter, X Salvatella, M Vendruscolo

J Am Chem Soc

(2009)

131

3810

(doi: 10.1021/ja8087295)

The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints

CT Friel, DA Smith, M Vendruscolo, J Gsponer, SE Radford

Nat Struct Mol Biol

(2009)

16

318

(doi: 10.1038/nsmb.1562)

Factors that affect the degree of twist in β-sheet structures: A Molecular dynamics simulation study of a cross-β filament of the GNNQQNY peptide

X Periole, A Rampioni, M Vendruscolo, AE Mark

J Phys Chem B

(2009)

113

1728

(doi: 10.1021/jp8078259)

Similarities in the thermodynamics and kinetics of aggregation of disease-related Aβ(1-40) peptides

J Meinhardt, GG Tartaglia, A Pawar, T Christopeit, P Hortschansky, V Schroeckh, CM Dobson, M Vendruscolo, M Fändrich

Protein Science

(2009)

16

1214

(doi: 10.1110/ps.062734207)

Molecular determinants of the aggregation behavior of alpha- and beta-synuclein

RC Rivers, JR Kumita, GG Tartaglia, MM Dedmon, A Pawar, M Vendruscolo, CM Dobson, J Christodoulou

Protein science : a publication of the Protein Society

(2009)

17

887

(doi: 10.1110/ps.073181508)

Competition between Folding, Native-State Dimerisation and Amyloid Aggregation in β-Lactoglobulin

D Hamada, T Tanaka, GG Tartaglia, A Pawar, M Vendruscolo, M Kawamura, A Tamura, N Tanaka, CM Dobson

J Mol Biol

(2008)

386

878

(doi: 10.1016/j.jmb.2008.12.038)

Self-Templated Nucleation in Peptide and Protein Aggregation

S Auer, CM Dobson, M Vendruscolo, A Maritan

Physical Review Letters

(2008)

101

258101

(doi: 10.1103/physrevlett.101.258101)

Determination of protein structures in the solid state from NMR chemical shifts.

P Robustelli, A Cavalli, M Vendruscolo

Structure (London, England : 1993)

(2008)

16

1764

(doi: 10.1016/j.str.2008.10.016)