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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

Structural Effects of Two Camelid Nanobodies Directed to Distinct C‑Terminal Epitopes on α‑Synuclein
F El-Turk, FN Newby, E De Genst, T Guilliams, T Sprules, A Mittermaier, CM Dobson, M Vendruscolo
– Biochemistry
(2016)
55,
3116
(doi: 10.1021/acs.biochem.6b00149)
Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.
C Camilloni, BM Sala, P Sormanni, R Porcari, A Corazza, M De Rosa, S Zanini, A Barbiroli, G Esposito, M Bolognesi, V Bellotti, M Vendruscolo, S Ricagno
– Scientific reports
(2016)
6,
25559
(doi: 10.1038/srep25559)
Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor.
A Deckert, CA Waudby, T Wlodarski, AS Wentink, X Wang, JP Kirkpatrick, JFS Paton, C Camilloni, P Kukic, CM Dobson, M Vendruscolo, LD Cabrita, J Christodoulou
– Proceedings of the National Academy of Sciences of the United States of America
(2016)
113,
5012
(doi: 10.1073/pnas.1519124113)
A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation
P Ciryam, R Kundra, R Freer, RI Morimoto, CM Dobson, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2016)
113,
4753
(doi: 10.1073/pnas.1516604113)
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.
P Arosio, TCT Michaels, S Linse, C Månsson, C Emanuelsson, J Presto, J Johansson, M Vendruscolo, CM Dobson, TPJ Knowles
– Nature Communications
(2016)
7,
10948
(doi: 10.1038/ncomms10948)
Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain
D Bonetti, C Camilloni, L Visconti, S Longhi, M Brunori, M Vendruscolo, S Gianni
– J Biol Chem
(2016)
291,
10886
(doi: 10.1074/jbc.M116.721126)
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.
P Joshi, S Chia, J Habchi, TPJ Knowles, CM Dobson, M Vendruscolo
– ACS Combinatorial Science
(2016)
18,
144
(doi: 10.1021/acscombsci.5b00129)
A structural ensemble of a ribosome–nascent chain complex during cotranslational protein folding
LD Cabrita, AME Cassaignau, HMM Launay, CA Waudby, T Wlodarski, C Camilloni, M-E Karyadi, AL Robertson, X Wang, AS Wentink, L Goodsell, CA Woolhead, M Vendruscolo, CM Dobson, J Christodoulou
– Nat Struct Mol Biol
(2016)
23,
278
(doi: 10.1038/nsmb.3182)
Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein.
A Toto, C Camilloni, R Giri, M Brunori, M Vendruscolo, S Gianni
– Scientific Reports
(2016)
6,
21994
(doi: 10.1038/srep21994)
Neuroscience: An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Ab42 aggregates linked with Alzheimer's disease
J Habchi, P Arosio, M Perni, AR Costa, M Yagi-Utsumi, P Joshi, S Chia, SIA Cohen, MBD Müller, S Linse, EAA Nollen, CM Dobson, TPJ Knowles, M Vendruscolo
– Science advances
(2016)
2,
e1501244
(doi: 10.1126/sciadv.1501244)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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