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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

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
(2021)
118,
e2103015118
Identification of a Thyroid Hormone Derivative as a Pleiotropic Agent for the Treatment of Alzheimer's Disease.
M Runfola, M Perni, X Yang, M Marchese, A Bacci, S Mero, FM Santorelli, B Polini, G Chiellini, D Giuliani, A Vilella, M Bodria, E Daini, E Vandini, S Rudge, S Gul, MOJ Wakelam, M Vendruscolo, S Rapposelli
– Pharmaceuticals (Basel)
(2021)
14,
1330
Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation.
J West, S Satapathy, DR Whiten, M Kelly, NJ Geraghty, E-J Proctor, P Sormanni, M Vendruscolo, JN Buxbaum, M Ranson, MR Wilson
– Science Advances
(2021)
7,
eabf7606
A structural ensemble of a tau-microtubule complex reveals regulatory tau phosphorylation and acetylation mechanisms
F Brotzakis, P Lindstedt, R Taylor, G Bernardes, M Vendruscolo
– ACS Central Science
(2021)
A Structural Ensemble of a Tau-Microtubule Complex Reveals Regulatory Tau Phosphorylation and Acetylation Mechanisms
ZF Brotzakis, PR Lindstedt, RJ Taylor, DJ Rinauro, NCT Gallagher, GJL Bernardes, M Vendruscolo
– ACS central science
(2021)
7,
1986
Structure-based discovery of small molecule inhibitors of the autocatalytic proliferation of α-synuclein aggregates
S Chia, ZF Brotzakis, RI Horne, A Possenti, B Mannini, R Cataldi, M Nowinska, R Staats, S Linse, TPJ Knowles, J Habchi, M Vendruscolo
(2021)
Proliferation of Tau 304-380 Fragment Aggregates through Autocatalytic Secondary Nucleation.
DC Rodriguez Camargo, E Sileikis, S Chia, E Axell, K Bernfur, RL Cataldi, SIA Cohen, G Meisl, J Habchi, TPJ Knowles, M Vendruscolo, S Linse
– ACS chemical neuroscience
(2021)
12,
4406
Discovery of Potent Inhibitors of α-Synuclein Aggregation Using Structure-Based Iterative Learning
R Horne, E Andrzejewska, P Alam, F Brotzakis, A Srivastava, A Aubert, M Nowinska, R Gregory, R Staats, A Possenti, S Chia, P Sormanni, B Ghetti, B Caughey, T Knowles, M Vendruscolo
(2021)
2021.11.10.468009
A small molecule stabilises the disordered native state of the Alzheimer’s Aβ peptide
T Löhr, K Kohlhoff, G Heller, C Camilloni, M Vendruscolo
(2021)
2021.11.10.468059
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement
M Vendruscolo, M Oeller, P Sormanni
– Scientific reports
(2021)
11,
21932
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk