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Centre for Misfolding Diseases

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


Targeted protein editing with an antibody-based system
M Vendruscolo, O Rimon, J Konc, M Ali, VR Chowdhury, P Sormanni, G Bernardes
Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.
DJ Rinauro, F Chiti, M Vendruscolo, R Limbocker
– Mol Neurodegener
Modulation of α-synuclein in vitro aggregation kinetics by its alternative splice isoforms
A Röntgen, Z Toprakcioglu, JE Tomkins, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils.
A Miller, S Chia, E Klimont, TPJ Knowles, M Vendruscolo, FS Ruggeri
– Commun Biol
Sequence-Based Drug Design Using Transformers
M Vendruscolo, S Zhang, D Huo, R Horne, Y Qi, SP Ojeda, A Yan
Imaging Aβ aggregation by liquid-phase transmission electron microscopy
G Ing, S Acosta-Gutiérrez, M Vendruscolo, G Battaglia, L Ruiz-Pérez
Transient interactions between the fuzzy coat and the cross-β core of brain-derived Aβ42 filaments
M Vendruscolo, M Milanesi, F Brotzakis
Using Generative Modeling to Endow with Potency Initially Inert Compounds with Good Bioavailability and Low Toxicity
RI Horne, J Wilson-Godber, A González Díaz, ZF Brotzakis, S Seal, RC Gregory, A Possenti, S Chia, M Vendruscolo
– Journal of chemical information and modeling
Transient interactions between the fuzzy coat and the cross-β core of brain-derived Aβ42 filaments
M Milanesi, F Brotzakis, M Vendruscolo
Aggregation of the Amyloid-β Peptide (Aβ40) within Condensates Generated through Liquid-Liquid Phase Separation
O Morris, Z Toprakcioglu, A Röntgen, M Cali, T Knowles, M Vendruscolo
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Telephone number

01223 763873

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