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Yusuf Hamied Department of Chemistry

 

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

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
– Proc Natl Acad Sci U S A
(2019)
117,
1015
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
– J Mol Biol
(2019)
432,
845
Determination of a Structural Ensemble Representing the Dynamics of a G‑Quadruplex DNA
G Portella, M Orozco, M Vendruscolo
– Biochemistry
(2019)
59,
379
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
(2019)
6,
137
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
(2019)
7,
197
Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis.
P Sormanni, M Vendruscolo
– Cold Spring Harbor Perspectives in Biology
(2019)
11,
a033845
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
R Limbocker, S Chia, FS Ruggeri, M Perni, R Cascella, GT Heller, G Meisl, B Mannini, J Habchi, TCT Michaels, PK Challa, M Ahn, ST Casford, N Fernando, CK Xu, ND Kloss, SIA Cohen, JR Kumita, C Cecchi, M Zasloff, S Linse, TPJ Knowles, F Chiti, M Vendruscolo, CM Dobson
– Nat Commun
(2019)
10,
225
Supersaturated proteins are enriched at synapses and underlie cell and tissue vulnerability in Alzheimer's disease
R Freer, P Sormanni, P Ciryam, B Rammner, SO Rizzoli, CM Dobson, M Vendruscolo
– Heliyon
(2019)
5,
e02589
Dynamics and Control of Peptide Self-Assembly and Aggregation
G Meisl, TCT Michaels, P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles
– Adv Exp Med Biol
(2019)
1174,
1
Million-fold sensitivity enhancement in proteopathic seed amplification assays for biospecimens by Hofmeister ion comparisons
MA Metrick, N do Carmo Ferreira, E Saijo, AG Hughson, A Kraus, C Orrú, MW Miller, G Zanusso, B Ghetti, M Vendruscolo, B Caughey
– Proceedings of the National Academy of Sciences of the United States of America
(2019)
116,
23029
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk