skip to content
Home

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

Molecular determinants of the interaction of EGCG with ordered and disordered proteins.
G Fusco, M Sanz-Hernandez, FS Ruggeri, M Vendruscolo, CM Dobson, A De Simone
– Biopolymers
(2018)
109,
e23117
(doi: 10.1002/bip.23117)
Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide.
SIA Cohen, R Cukalevski, TCT Michaels, A Šarić, M Törnquist, M Vendruscolo, CM Dobson, AK Buell, TPJ Knowles, S Linse
– Nature chemistry
(2018)
10,
523
(doi: 10.1038/s41557-018-0023-x)
Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation.
TCT Michaels, A Šarić, J Habchi, S Chia, G Meisl, M Vendruscolo, CM Dobson, TPJ Knowles
– Annual review of physical chemistry
(2018)
69,
1
(doi: 10.1146/annurev-physchem-050317-021322)
Molecular dynamics ensemble refinement of the heterogeneous native state of NCBD using chemical shifts and NOEs
E Papaleo, C Camilloni, K Teilum, M Vendruscolo, K Lindorff-Larsen
(2018)
273714
(doi: 10.1101/273714)
Systematic Development of Small Molecules to Inhibit Specific Microscopic Steps of Amyloid-Beta42 Aggregation in Alzheimer's Disease
S Chia, J Habchi, R Limbocker, B Mannini, M Ahn, M Perni, O Hansson, P Arosio, JR Kumita, PK Challa, SIA Cohen, S Linse, CM Dobson, TPJ Knowles, M Vendruscolo
– Biophysical Journal
(2018)
114,
225a
(doi: 10.1016/j.bpj.2017.11.1253)
Probing the Interaction of ABETA42 Amyloid Species with an Aggregation Suppressor Molecule by Infrared Nanospectroscopy
FS Ruggeri, J Habchi, S Chia, M Vendruscolo, TPJ Knowles
– Biophysical Journal
(2018)
114,
224a
(doi: 10.1016/j.bpj.2017.11.1246)
Principles of Protein Structural Ensemble Determination
M Vendruscolo
– Biophysical Journal
(2018)
114,
388A
(doi: 10.1016/j.bpj.2017.11.2149)
Modulating Amyloid-Beta Aggregation to Reduce the Toxicity of its Oligomeric Aggregates
R Limbocker, B Mannini, S Chia, FS Ruggeri, M Perni, R Cascella, C Xu, J Habchi, JR Kumita, F Chiti, TPJ Knowles, M Vendruscolo, CM Dobson
– Biophysical Journal
(2018)
114,
430A
(doi: 10.1016/j.bpj.2017.11.2382)
Third generation antibody discovery methods: in silico rational design.
P Sormanni, FA Aprile, M Vendruscolo
– Chemical Society Reviews
(2018)
47,
9137
(doi: 10.1039/c8cs00523k)
Systematic Development of Small Molecules to Inhibit Specific Steps of α-Synuclein Aggregation in Parkinson's Disease
R Staats, P Flagmeier, M Vendruscolo
– BIOPHYSICAL JOURNAL
(2018)
114,
77A
(link to publication)
  • <
  • 34 of 80
  • >

Research Groups

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk

    Study at Cambridge

    About the University

    Research at Cambridge