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 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
Proc Natl Acad Sci U S A
(2016)
113
(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
(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
(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
The Journal of biological chemistry
(2016)
291
(doi: 10.1074/jbc.m116.721126)
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
Nature Structural and Molecular Biology
(2016)
23
(doi: 10.1038/nsmb.3182)
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
(doi: 10.1021/acscombsci.5b00129)
Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein.
A Toto, C Camilloni, R Giri, M Brunori, M Vendruscolo, S Gianni
Sci Rep
(2016)
6
(doi: 10.1038/srep21994)
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 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
(doi: 10.1126/sciadv.1501244)
Hamiltonian Dynamics of Protein Filament Formation
TCT Michaels, SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
Phys Rev Lett
(2016)
116
(doi: 10.1103/physrevlett.116.038101)
Molecular mechanisms of protein aggregation from global fitting of kinetic models
G Meisl, JB Kirkegaard, P Arosio, TCT Michaels, M Vendruscolo, CM Dobson, S Linse, TPJ Knowles
Nature protocols
(2016)
11
(doi: 10.1038/nprot.2016.010)

Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk
Yusuf Hamied Department of Chemistry
Lensfield Road
Cambridge
CB2 1EW
T: +44 (0) 1223 336300
enquiries@ch.cam.ac.uk
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