Centre for Misfolding Diseases

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

Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop
AN Borkar, P Vallurupalli, C Camilloni, LE Kay, M Vendruscolo
Phys Chem Chem Phys
(2017)
19
(doi: 10.1039/c6cp08313g)
Networks of Dynamic Allostery Regulate Enzyme Function.
MJ Holliday, C Camilloni, GS Armstrong, M Vendruscolo, EZ Eisenmesser
Structure
(2017)
25
(doi: 10.1016/j.str.2016.12.003)
Principles of protein structural ensemble determination.
M Bonomi, GT Heller, C Camilloni, M Vendruscolo
Current Opinion in Structural Biology
(2017)
42
(doi: 10.1016/j.sbi.2016.12.004)
Structural characterisation of the early events in the nucleation-condensation mechanism of folding
P Kukic, Y Pustovalova, C Camilloni, S Gianni, DM Korzhnev, M Vendruscolo
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
Mechanisms of Amyloid-β 42 oligomer formation from kinetic analysis
TC Michaels, A Saric, HW Lazell, P Arosio, M Vendruscolo, CM Dobson, S Linse, TPJ Knowles
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
Single amyloid aggregates chemical and structural analysis by infrared nanospectroscopy
FS Ruggeri, J Habchi, C Sean, M Vendruscolo, TPJ Knowles
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease
J Habchi, S Chia, 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
Proc Natl Acad Sci U S A
(2016)
114
(doi: 10.1073/pnas.1615613114)
β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces
JWP Brown, AK Buell, TCT Michaels, G Meisl, J Carozza, P Flagmeier, M Vendruscolo, TPJ Knowles, CM Dobson, C Galvagnion
Scientific reports
(2016)
6
(doi: 10.1038/srep36010)
Structural basis of synaptic vesicle assembly promoted by α-synuclein
G Fusco, T Pape, AD Stephens, P Mahou, AR Costa, CF Kaminski, GS Kaminski Schierle, M Vendruscolo, G Veglia, CM Dobson, A De Simone
Nat Commun
(2016)
7
(doi: 10.1038/ncomms12563)
Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation.
P Flagmeier, G Meisl, M Vendruscolo, TPJ Knowles, CM Dobson, AK Buell, C Galvagnion
Proceedings of the National Academy of Sciences of the United States of America
(2016)
113
(doi: 10.1073/pnas.1604645113)

Co-Director

Research Interest Groups

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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