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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


Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH.
ST Dada, MC Hardenberg, Z Toprakcioglu, LK Mrugalla, MP Cali, MO McKeon, E Klimont, TCT Michaels, TPJ Knowles, M Vendruscolo
– Proceedings of the National Academy of Sciences
Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes
T Bhardwaj, K Gadhave, SK Kapuganti, P Kumar, ZF Brotzakis, KU Saumya, N Nayak, A Kumar, R Joshi, B Mukherjee, A Bhardwaj, KG Thakur, N Garg, M Vendruscolo, R Giri
– Nature Communications
Combinations of Vitamin A and Vitamin E Metabolites Confer Resilience against Amyloid‑β Aggregation
P Joshi, S Chia, X Yang, M Perni, JM Gabriel, M Gilmer, R Limbocker, J Habchi, M Vendruscolo
– ACS Chemical Neuroscience
Sequence-based prediction of pH-dependent protein solubility using CamSol
M Oeller, R Kang, R Bell, H Ausserwöger, P Sormanni, M Vendruscolo
– Briefings in Bioinformatics
AlphaFold Prediction of Structural Ensembles of Disordered Proteins
F Brotzakis, S Zhang, M Vendruscolo
Enhanced surface nanoanalytics of transient biomolecular processes
AM Miller, S Chia, Z Toprakcioglo, T Hakala, R Schmid, Y Feng, T Kartanas, A Kamada, M Vendruscolo, FS Ruggeri, T Knowles
– Science Advances
A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ42 Aggregation
KN Baumann, G Šneiderienė, M Sanguanini, M Schneider, O Rimon, A González Díaz, H Greer, D Thacker, S Linse, TPJ Knowles, M Vendruscolo
– ACS chemical neuroscience
Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates
S Chia, Z Faidon Brotzakis, RI Horne, A Possenti, B Mannini, R Cataldi, M Nowinska, R Staats, S Linse, TPJ Knowles, J Habchi, M Vendruscolo
– Molecular Pharmaceutics
Fragment-based computational design of antibodies targeting structured epitopes.
M Aguilar Rangel, A Bedwell, E Costanzi, RJ Taylor, R Russo, GJL Bernardes, S Ricagno, J Frydman, M Vendruscolo, P Sormanni
– Science Advances
Sequence-based Prediction of the Cellular Toxicity Associated with Amyloid Aggregation within Protein Condensates
A Horvath, M Vendruscolo, M Fuxreiter
– Biochemistry
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Research Interest Groups

Telephone number

01223 763873

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