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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

The Hsc70 Disaggregation Machinery Removes Monomer Units Directly from α-Synuclein Fibril Ends
M Schneider, S Gautam, T Herling, E Andrzejewska, G Krainer, A Miller, Q Peter, FS Ruggeri, M Vendruscolo, A Bracher, C Dobson, U Hartl, T Knowles
(2020)
2020.11.02.365825
(doi: 10.1101/2020.11.02.365825)
An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase.
AE Conicella, R Huang, ZA Ripstein, A Nguyen, E Wang, T Löhr, P Schuck, M Vendruscolo, JL Rubinstein, LE Kay
– Proc Natl Acad Sci U S A
(2020)
117,
26226
(doi: 10.1073/pnas.2013920117)
Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies
S Linse, T Scheidt, K Bernfur, M Vendruscolo, CM Dobson, SIA Cohen, E Sileikis, M Lundqvist, F Qian, T O'Malley, T Bussiere, PH Weinreb, CK Xu, G Meisl, SRA Devenish, TPJ Knowles, O Hansson
– Nature Structural & Molecular Biology
(2020)
27,
1125
(doi: 10.1038/s41594-020-0505-6)
A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease
T Ikenoue, FA Aprile, P Sormanni, FS Ruggeri, M Perni, GT Heller, CP Haas, C Middel, R Limbocker, B Mannini, TCT Michaels, TPJ Knowles, CM Dobson, M Vendruscolo
– Scientific Reports
(2020)
10,
15280
(doi: 10.1038/s41598-020-69626-3)
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.
TCT Michaels, A Šarić, G Meisl, GT Heller, S Curk, P Arosio, S Linse, CM Dobson, M Vendruscolo, TPJ Knowles
– Proceedings of the National Academy of Sciences of the United States of America
(2020)
117,
24251
(doi: 10.1073/pnas.2006684117)
Kinetic analysis reveals the rates and mechanisms of protein aggregation in a multicellular organism
T Sinnige, G Meisl, T Michaels, M Vendruscolo, TPJ Knowles, R Morimoto
(2020)
2020.08.13.249862
(doi: 10.1101/2020.08.13.249862)
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism.
R Limbocker, B Mannini, FS Ruggeri, R Cascella, CK Xu, M Perni, S Chia, SW Chen, J Habchi, A Bigi, RP Kreiser, AK Wright, JA Albright, T Kartanas, JR Kumita, N Cremades, M Zasloff, C Cecchi, TPJ Knowles, F Chiti, M Vendruscolo, CM Dobson
– Communications biology
(2020)
3,
435
(doi: 10.1038/s42003-020-01140-8)
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation.
P Flagmeier, S De, TCT Michaels, X Yang, AJ Dear, C Emanuelsson, M Vendruscolo, S Linse, D Klenerman, TPJ Knowles, CM Dobson
– Nature Structural and Molecular Biology
(2020)
27,
886
(doi: 10.1038/s41594-020-0471-z)
Rationally Designed Antibodies as Research Tools to Study the Structure–Toxicity Relationship of Amyloid-β Oligomers
R Limbocker, B Mannini, R Cataldi, S Chhangur, AK Wright, RP Kreiser, JA Albright, S Chia, J Habchi, P Sormanni, JR Kumita, FS Ruggeri, CM Dobson, F Chiti, FA Aprile, M Vendruscolo
– International Journal of Molecular Sciences
(2020)
21,
E4542
(doi: 10.3390/ijms21124542)
Infrared Nanospectroscopy Reveals the Molecular Interaction Fingerprint of an Aggregation Inhibitor with Single Aβ42 Oligomers
FS Ruggeri, J Habchi, S Chia, M Vendruscolo, T Knowles
(2020)
(doi: 10.1101/2020.06.24.168997)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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