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Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

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

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)
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 (vol 113, pg 1728, 2009)
X Periole, A Rampioni, M Vendruscolo, AE Mark
– The Journal of Physical Chemistry B
(2009)
113,
10548
(doi: 10.1021/jp905822d)
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 (Journal of Physical Chemistry B (2009) 113B (1728))
X Periole, A Rampioni, M Vendruscolo, AE Mark
– Journal of Physical Chemistry B
(2009)
113,
10548
(doi: 10.1021/jp905822d)
Towards quantitative predictions in cell biology using chemical properties of proteins
M Vendruscolo
– FEBS JOURNAL
(2009)
276,
12
(link to publication)
Competition between Intramolecular and Intermolecular Interactions in an Amyloid-Forming Protein
KE Routledge, GG Tartaglia, GW Platt, M Vendrusco, SE Radford
– Journal of Molecular Biology
(2009)
389,
776
(doi: 10.1016/j.jmb.2009.04.042)
Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins
S Pechmann, ED Levy, GG Tartaglia, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2009)
106,
10159
(doi: 10.1073/pnas.0812414106)
Position-Dependent Electrostatic Protection against Protein Aggregation
AK Buell, GG Tartaglia, NR Birkett, CA Waudby, M Vendruscolo, X Salvatella, ME Welland, CM Dobson, TPJ Knowles
– ChemBioChem
(2009)
10,
1309
(doi: 10.1002/cbic.200900144)
Physical principles of protein behavior in the cell
M Porto, HE Roman, M Vendruscolo
– Journal of proteome research
(2009)
8,
2615
(doi: 10.1021/pr900340d)
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
– J Phys Chem B
(2009)
113,
7890
(doi: 10.1021/jp900780b)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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