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Yusuf Hamied Department of Chemistry

Portrait of mv245

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


A small molecule stabilises the disordered native state of the Alzheimer’s Aβ peptide
T Löhr, K Kohlhoff, G Heller, C Camilloni, M Vendruscolo
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement
M Oeller, P Sormanni, M Vendruscolo
– Sci Rep
Vitamin A and vitamin E metabolites comodulate amyloid-β aggregation
P Joshi, S Chia, X Yang, M Perni, J Habchi, M Vendruscolo
Surface-Catalyzed Secondary Nucleation Dominates the Generation of Toxic IAPP Aggregates.
DC Rodriguez Camargo, S Chia, J Menzies, B Mannini, G Meisl, M Lundqvist, C Pohl, K Bernfur, V Lattanzi, J Habchi, SI Cohen, TPJ Knowles, M Vendruscolo, S Linse
– Front Mol Biosci
The signal peptide of the amyloid precursor protein forms amyloid-like aggregates and enhances A beta 42 aggregation
K Gadhave, T Bhardwaj, VN Uversky, M Vendruscolo, R Giri
– Cell Reports Physical Science
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends
MM Schneider, S Gautam, TW Herling, E Andrzejewska, G Krainer, AM Miller, VA Trinkaus, QAE Peter, FS Ruggeri, M Vendruscolo, A Bracher, CM Dobson, FU Hartl, TPJ Knowles
– Nature communications
The cellular modifier MOAG‐4/SERF drives amyloid formation through charge complementation
A Pras, B Houben, FA Aprile, R Seinstra, R Gallardo, L Janssen, W Hogewerf, C Gallrein, M De Vleeschouwer, A Mata-Cabana, M Koopman, E Stroo, M de Vries, S Louise Edwards, J Kirstein, M Vendruscolo, SF Falsone, F Rousseau, J Schymkowitz, EAA Nollen
– The EMBO Journal
New frontiers for machine learning in protein science
AS Morgunov, KL Saar, M Vendruscolo, TPJ Knowles
– J Mol Biol
A maximum caliber approach for continuum path ensembles
PG Bolhuis, ZF Brotzakis, M Vendruscolo
– European Physical Journal B
The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces
T Scheidt, JA Carozza, CC Kolbe, FA Aprile, O Tkachenko, MMJ Bellaiche, G Meisl, QAE Peter, TW Herling, S Ness, M Castellana-Cruz, JLP Benesch, M Vendruscolo, CM Dobson, P Arosio, TPJ Knowles
– Proceedings of the National Academy of Sciences of the United States of America
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Research Interest Groups

Telephone number

01223 763873

Email address