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

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
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
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
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
Hamiltonian Dynamics of Protein Filament Formation
TCT Michaels, SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
Physical Review Letters
(2016)
116
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
Metainference: A Bayesian inference method for heterogeneous systems.
M Bonomi, C Camilloni, A Cavalli, M Vendruscolo
Science advances
(2016)
2
Structural Insights into the Calcium-Mediated Allosteric Transition in the C-Terminal Domain of Calmodulin from Nuclear Magnetic Resonance Measurements.
P Kukic, P Lundström, C Camilloni, J Evenäs, M Akke, M Vendruscolo
Biochemistry
(2015)
55
Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.
P Arosio, T Müller, L Rajah, EV Yates, FA Aprile, Y Zhang, SIA Cohen, DA White, TW Herling, EJ De Genst, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles
ACS Nano
(2015)
10
Using Pseudocontact Shifts and Residual Dipolar Couplings as Exact NMR Restraints for the Determination of Protein Structural Ensembles
C Camilloni, M Vendruscolo
Biochemistry
(2015)
54

Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address