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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

Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation.

G Calloni, C Lendel, S Campioni, S Giannini, A Gliozzi, A Relini, M Vendruscolo, CM Dobson, X Salvatella, F Chiti

– J Am Chem Soc

(2008)

130,

13040

(doi: 10.1021/ja8029224)

Towards quantitative predictions in cell biology using chemical properties of proteins

M Vendruscolo, GG Tartaglia

– Molecular Biosystems

(2008)

4,

1170

(doi: 10.1039/b805710a)

Prediction by graph theoretic measures of structural effects in proteins arising from non-synonymous single nucleotide polymorphisms.

TMK Cheng, Y-E Lu, M Vendruscolo, P Lio', TL Blundell

– PLOS Computational Biology

(2008)

4,

e1000135

(doi: 10.1371/journal.pcbi.1000135)

Characterizing the first steps of amyloid formation for the ccβ peptide

B Strodel, AW Fitzpatrick, M Vendruscolo, CM Dobson, DJ Wales

– J Phys Chem B

(2008)

112,

9998

(doi: 10.1021/jp801222x)

Mapping of two networks of residues that exhibit structural and dynamical changes upon binding in a PDZ domain protein.

A Dhulesia, J Gsponer, M Vendruscolo

– J Am Chem Soc

(2008)

130,

8931

(doi: 10.1021/ja0752080)

A stochastic method for the reconstruction of protein structures from one-dimensional structural profiles

K Wolff, M Vendruscolo, M Porto

– Gene

(2008)

422,

47

(doi: 10.1016/j.gene.2008.06.004)

The Zyggregator method for predicting protein aggregation propensities.

GG Tartaglia, M Vendruscolo

– Chem Soc Rev

(2008)

37,

1395

(doi: 10.1039/b706784b)

Prediction of aggregation-prone regions in structured proteins

GG Tartaglia, AP Pawar, S Campioni, CM Dobson, F Chiti, M Vendruscolo

– Journal of molecular biology

(2008)

380,

425

(doi: 10.1016/j.jmb.2008.05.013)

A Coupled Equilibrium Shift Mechanism in Calmodulin-Mediated Signal Transduction

J Gsponer, J Christodoulou, A Cavalli, JM Bui, B Richter, CM Dobson, M Vendruscolo

– Structure

(2008)

16,

736

(doi: 10.1016/j.str.2008.02.017)

Calculation of the free energy barriers in the oligomerisation of A beta peptide fragments

M Cheon, G Favrin, I Chang, CM Dobson, M Vendruscolo

– Frontiers in Bioscience

(2008)

13,

5614

(doi: 10.2741/3104)