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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

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

(2008)

16,

1764

(doi: 10.1016/j.str.2008.10.016)

Stochastic reconstruction of protein structures from effective connectivity profiles

K Wolff, M Vendruscolo, M Porto

– PMC Biophys

(2008)

1,

5

(doi: 10.1186/1757-5036-1-5)

Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins.

N Calosci, CN Chi, B Richter, C Camilloni, A Engström, L Eklund, C Travaglini-Allocatelli, S Gianni, M Vendruscolo, P Jemth

– Proceedings of the National Academy of Sciences of the United States of America

(2008)

105,

19241

(doi: 10.1073/pnas.0804774105)

A Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric Aggregates

S Auer, F Meersman, CM Dobson, M Vendruscolo

– PLOS Computational Biology

(2008)

4,

e1000222

(doi: 10.1371/journal.pcbi.1000222)

Structure determination of protein-protein complexes using NMR chemical shifts: Case of an endonuclease colicin-immunity protein complex

RW Montalvao, A Cavalli, X Salvatella, TL Blundell, M Vendruscolo

– Journal of the American Chemical Society

(2008)

130,

15990

(doi: 10.1021/ja805258z)

Competition between protein aggregation and protein complex formation

S Pechmann, ED Levy, GG Tartaglia, M Vendruscolo

– BMC Bioinformatics

(2008)

9,

o2

(doi: 10.1186/1471-2105-9-S10-O2)

Inhibition of alpha-Synuclein Fibrillization by Dopamine Is Mediated by Interactions with Five C-Terminal Residues and with E83 in the NAC Region

FE Herrera, A Chesi, KE Paleologou, A Schmid, A Munoz, M Vendruscolo, S Gustincich, HA Lashuel, P Carloni

– PloS one

(2008)

3,

e3394

(doi: 10.1371/journal.pone.0003394)

Physical and Chemical Foundations of Bioinformatics Methods

M Porto, HE Roman, M Vendruscolo

– Gene

(2008)

422,

vii

(doi: 10.1016/j.gene.2008.06.001)

Introduction to the special issue of GENE

M Porto, HE Roman, M Vendruscolo

– Gene

(2008)

422,

7

(doi: 10.1016/j.gene.2008.06.001)