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Professor Michele Vendruscolo

Portrait of mv245


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.

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.




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, GS Schierle, E Rees, A Miyashita, AR Costa, RB Dodd, FT Chan, CH Michel, D Kronenberg-Versteeg, Y Li, SP Yang, Y Wakutani, W Meadows, RR Ferry, L Dong, GG Tartaglia, G Favrin, WL 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)
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)
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, TP Knowles – Nature Chemistry (2015) 7, 802
Mapping the Protein Fold Universe Using the CamTube Force Field in Molecular Dynamics Simulations.
P Kukic, A Kannan, MJ Dijkstra, S Abeln, C Camilloni, M Vendruscolo – PLoS computational biology (2015) 11, e1004435
Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates
MA Wright, FA Aprile, P Arosio, M Vendruscolo, CM Dobson, TP Knowles – Chemical communications (Cambridge, England) (2015) 51, 14425
Targeting disordered proteins with small molecules using entropy
GT Heller, P Sormanni, M Vendruscolo – Trends in Biochemical Sciences (2015) 40, 491
Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins
P Sormanni, FA Aprile, M Vendruscolo – Proceedings of the National Academy of Sciences of the United States of America (2015) 112, 9902
A Rational Design Strategy for the Selective Activity Enhancement of a Molecular Chaperone toward a Target Substrate.
FA Aprile, P Sormanni, M Vendruscolo – Biochemistry (2015) 54, 5103
Chromatin Unfolding by Epigenetic Modifications Explained by Dramatic Impairment of Internucleosome Interactions: A Multiscale Computational Study
R Collepardo-Guevara, G Portella, M Vendruscolo, D Frenkel, T Schlick, M Orozco – Journal of the American Chemical Society (2015) 137, 10205
Probing the Residual Structure of the Low Populated Denatured State of ADA2h under Folding Conditions by Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy
Y Pustovalova, P Kukic, M Vendruscolo, DM Korzhnev – Biochemistry (2015) 54, 4611
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01223 763873

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