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Department of Chemistry

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.




The N-terminal Acetylation of α-Synuclein Changes the Affinity for Lipid Membranes but not the Structural Properties of the Bound State
M Runfola, A De Simone, M Vendruscolo, CM Dobson, G Fusco
– Scientific Reports
Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers
SA Ghadami, S Chia, FS Ruggeri, G Meisl, F Bemporad, J Habchi, R Cascella, CM Dobson, M Vendruscolo, TPJ Knowles, F Chiti
– Biomacromolecules
Chris Dobson (1949-2019).
TPJ Knowles, M Vendruscolo
– Nature chemical biology
Widespread remodeling of proteome solubility in response to different protein homeostasis stresses.
X Sui, DEV Pires, AR Ormsby, D Cox, S Nie, G Vecchi, M Vendruscolo, DB Ascher, GE Reid, DM Hatters
– Proc Natl Acad Sci U S A
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
T Michaels, A Šarić, S Curk, K Bernfur, P Arosio, G Meisl, A Dear, S Cohen, M Vendruscolo, C Dobson, S Linse, T Knowles
Proteome-wide observation of the phenomenon of life on the edge of solubility.
G Vecchi, P Sormanni, B Mannini, A Vandelli, GG Tartaglia, CM Dobson, FU Hartl, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
Inherent Biophysical Properties Modulate the Toxicity of Soluble Amyloidogenic Light Chains.
M Maritan, M Romeo, L Oberti, P Sormanni, M Tasaki, R Russo, A Ambrosetti, P Motta, P Rognoni, G Mazzini, A Barbiroli, G Palladini, M Vendruscolo, L Diomede, M Bolognesi, G Merlini, F Lavatelli, S Ricagno
– Journal of molecular biology
Homage to Chris Dobson
J Baum, F Chiti, A De Simone, TPJ Knowles, JR Kumita, SE Radford, CV Robinson, X Salvatella, K Valelli, M Vendruscolo, A Pastore, GG Tartaglia
– Frontiers in Molecular Biosciences
Determination of a Structural Ensemble Representing the Dynamics of a G-Quadruplex DNA
G Portella, M Orozco, M Vendruscolo
– Biochemistry
A metastable subproteome underlies inclusion formation in muscle proteinopathies
P Ciryam, M Antalek, F Cid, GG Tartaglia, CM Dobson, A-K Guettsches, B Eggers, M Vorgerd, K Marcus, RA Kley, RI Morimoto, M Vendruscolo, CC Weihl
– Acta Neuropathol Commun
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01223 763873

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