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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


A Small Molecule Stabilizes the Disordered Native State of the Alzheimer's Aβ Peptide.
T Löhr, K Kohlhoff, GT Heller, C Camilloni, M Vendruscolo
– ACS Chem Neurosci
Determination of the structure and dynamics of the fuzzy coat of an amyloid fibril of IAPP using cryo-electron microscopy
F Brotzakis, T Löhr, S Truong, S Hoff, M Bonomi, M Vendruscolo
FuzDrop on AlphaFold: visualizing the sequence-dependent propensity of liquid-liquid phase separation and aggregation of proteins
A Hatos, SCE Tosatto, M Vendruscolo, M Fuxreiter
– Nucleic Acids Res
Conformational Entropy as a Potential Liability of Computationally Designed Antibodies
T Löhr, P Sormanni, M Vendruscolo
– Biomolecules
Kinetic profiling of therapeutic strategies for inhibiting the formation of amyloid oligomers.
TCT Michaels, AJ Dear, SIA Cohen, M Vendruscolo, TPJ Knowles
– J Chem Phys
A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents.
RP Kreiser, AK Wright, LR Sasser, DJ Rinauro, JM Gabriel, CM Hsu, JA Hurtado, TL McKenzie, S Errico, JA Albright, L Richardson, VA Jaffett, DE Riegner, LT Nguyen, K LeForte, M Zasloff, JE Hollows, F Chiti, M Vendruscolo, R Limbocker
– ACS Chem Neurosci
A Machine Learning Approach to Identify Small Molecule Inhibitors of Secondary Nucleation in α-Synuclein Aggregation
R Horne, A Possenti, S Chia, F Brotzakis, R Staats, M Nowinska, M Vendruscolo
Sequence Determinants of the Aggregation of Proteins Within Condensates Generated by Liquid-liquid Phase Separation: Sequence code of aggregation in protein condensates
M Vendruscolo, M Fuxreiter
– Journal of molecular biology
Squalamine and trodusquemine: two natural products for neurodegenerative diseases, from physical chemistry to the clinic
R Limbocker, S Errico, D Barbut, TPJ Knowles, M Vendruscolo, F Chiti, M Zasloff
– Natural product reports
Common sequence motifs of nascent chains engage the ribosome surface and trigger factor
A Deckert, AME Cassaignau, X Wang, T Włodarski, SHS Chan, CA Waudby, JP Kirkpatrick, M Vendruscolo, LD Cabrita, J Christodoulou
– Proc Natl Acad Sci U S A
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Telephone number

01223 763873

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