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

Parmbsc1: a refined force field for DNA simulations
I Ivani, PD Dans, A Noy, A Pérez, I Faustino, A Hospital, J Walther, P Andrio, R Goñi, A Balaceanu, G Portella, F Battistini, JL Gelpí, C González, M Vendruscolo, CA Laughton, SA Harris, DA Case, M Orozco
Nat Methods
(2015)
13
Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins
FN Newby, A De Simone, M Yagi-Utsumi, X Salvatella, CM Dobson, M Vendruscolo
Biochemistry
(2015)
54
ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function.
T Murakami, S Qamar, JQ Lin, GSK Schierle, E Rees, A Miyashita, AR Costa, RB Dodd, FTS Chan, CH Michel, D Kronenberg-Versteeg, Y Li, S-P Yang, Y Wakutani, W Meadows, RR Ferry, L Dong, GG Tartaglia, G Favrin, W-L Lin, DW Dickson, M Zhen, D Ron, G Schmitt-Ulms, PE Fraser, NA Shneider, C Holt, M Vendruscolo, CF Kaminski, P St George-Hyslop
Neuron
(2015)
88
Mapping the Protein Fold Universe Using the CamTube Force Field in Molecular Dynamics Simulations
P Kukic, A Kannan, MJJ Dijkstra, S Abeln, C Camilloni, M Vendruscolo
PLOS Computational Biology
(2015)
11
The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments
D Granata, F Baftizadeh, J Habchi, C Galvagnion, A De Simone, C Camilloni, A Laio, M Vendruscolo
Sci Rep
(2015)
5
ChemInform Abstract: Biophysical Approaches for the Study of Interactions Between Molecular Chaperones and Protein Aggregates
MA Wright, FA Aprile, P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles
ChemInform
(2015)
46
Particle-based simulations of steady-state mass transport at high Péclet numbers
T Müller, P Arosio, L Rajah, SIA Cohen, EV Yates, M Vendruscolo, CM Dobson, TPJ Knowles
(2015)
Particle-based simulations of steady-state mass transport at high Péclet numbers
T Müller, P Arosio, L Rajah, SIA Cohen, EV Yates, M Vendruscolo, CM Dobson, TPJ Knowles
(2015)
Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity.
EV Yates, T Müller, L Rajah, EJ De Genst, P Arosio, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles
Nature Chemistry
(2015)
7
Druggability of Intrinsically Disordered Proteins.
P Joshi, M Vendruscolo
Advances in Experimental Medicine and Biology
(2015)
870

Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address