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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

Complexity in Lipid Membrane Composition Induces Resilience to Aβ42 Aggregation
M Sanguanini, KN Baumann, S Preet, S Chia, J Habchi, TPJ Knowles, M Vendruscolo
– ACS Chemical Neuroscience
(2020)
11,
1347
(doi: 10.1021/acschemneuro.0c00101)
Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide (Nature Chemistry, (2020), 12, 5, (445-451), 10.1038/s41557-020-0452-1)
TCT Michaels, A Šarić, S Curk, K Bernfur, P Arosio, G Meisl, AJ Dear, SIA Cohen, CM Dobson, M Vendruscolo, S Linse, TPJ Knowles
– Nat Chem
(2020)
12,
497
(doi: 10.1038/s41557-020-0468-6)
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
TCT Michaels, A Šarić, S Curk, K Bernfur, P Arosio, G Meisl, AJ Dear, SIA Cohen, CM Dobson, M Vendruscolo, S Linse, TPJ Knowles
– Nature Chemistry
(2020)
12,
445
(doi: 10.1038/s41557-020-0452-1)
Sequence-Based Prediction of Fuzzy Protein Interactions
M Miskei, A Horvath, M Vendruscolo, M Fuxreiter
– J Mol Biol
(2020)
432,
2289
(doi: 10.1016/j.jmb.2020.02.017)
A Cell- and Tissue-Specific Weakness of the Protein Homeostasis System Underlies Brain Vulnerability to Protein Aggregation
R Kundra, CM Dobson, M Vendruscolo
– iScience
(2020)
23,
100934
(doi: 10.1016/j.isci.2020.100934)
A single ultrasensitive assay for detection and discrimination of tau aggregates of Alzheimer and Pick diseases.
MA Metrick, NDC Ferreira, E Saijo, A Kraus, K Newell, G Zanusso, M Vendruscolo, B Ghetti, B Caughey
– Acta neuropathologica communications
(2020)
8,
22
(doi: 10.1186/s40478-020-0887-z)
Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers
SA Ghadami, S Chia, FS Ruggeri, G Meisl, F Bemporad, J Habchi, R Cascella, CM Dobson, M Vendruscolo, TPJ Knowles, F Chiti
– Biomacromolecules
(2020)
21,
1112
(doi: 10.1021/acs.biomac.9b01475)
The amyloid phenomenon and its significance in biology and medicine
CM Dobson, TPJ Knowles, M Vendruscolo
– Cold Spring Harbor perspectives in biology
(2020)
12,
a033878
(doi: 10.1101/cshperspect.a033878)
A Role of Cholesterol in Modulating the Binding of α-Synuclein to Synaptic-Like Vesicles.
WK Man, A De Simone, JD Barritt, M Vendruscolo, CM Dobson, G Fusco
– Frontiers in neuroscience
(2020)
14,
18
(doi: 10.3389/fnins.2020.00018)
Chris Dobson (1949–2019)
TPJ Knowles, M Vendruscolo
– Nature Chemical Biology
(2020)
16,
105
(doi: 10.1038/s41589-019-0456-6)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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