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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

Determination of intermediate state structures in the opening pathway of SARS-CoV-2 spike using cryo-electron microscopy.
ZF Brotzakis, T Löhr, M Vendruscolo
– Chem Sci
(2021)
12,
9168
Critical assessment of protein intrinsic disorder prediction.
M Necci, D Piovesan, CAID Predictors, DisProt Curators, SCE Tosatto
– Nature Methods
(2021)
18,
472
A mistranslation-prone transcriptome underlying polyglutamine expansion diseases
F Buhr, PS Ciryam, M Vendruscolo
– Nature reviews. Molecular cell biology
(2021)
22,
583
Tau AD fragment aggregates proliferate through autocatalytic secondary nucleation
DR Camargo, E Sileikis, S Chia, E Axell, K Bernfur, R Cataldi, S Cohen, G Meisl, J Habchi, T Knowles, M Vendruscolo, S Linse
(2021)
Comparative Studies in the A30P and A53T α-Synuclein C. elegans Strains to Investigate the Molecular Origins of Parkinson's Disease.
M Perni, A van der Goot, R Limbocker, TJ van Ham, FA Aprile, CK Xu, P Flagmeier, K Thijssen, P Sormanni, G Fusco, SW Chen, PK Challa, JB Kirkegaard, RF Laine, KY Ma, MBD Müller, T Sinnige, JR Kumita, SIA Cohen, R Seinstra, GS Kaminski Schierle, CF Kaminski, D Barbut, A De Simone, TPJ Knowles, M Zasloff, EAA Nollen, M Vendruscolo, CM Dobson
– Frontiers in cell and developmental biology
(2021)
9,
552549
Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans
T Sinnige, G Meisl, TCT Michaels, M Vendruscolo, TPJ Knowles, RI Morimoto
– Proceedings of the National Academy of Sciences
(2021)
118,
e2021888118
Fragment-based computational design of antibodies targeting structured epitopes
MA Rangel, A Bedwell, E Costanzi, R Taylor, R Russo, G Bernardes, S Ricagno, J Frydman, M Vendruscolo, P Sormanni
(2021)
2021.03.02.433360
Rationally designed bicyclic peptides prevent the conversion of Aβ42 assemblies into fibrillar structures
T Ikenoue, FA Aprile, P Sormanni, M Vendruscolo
– Frontiers in Neuroscience
(2021)
15,
623097
Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.
K Kulenkampff, A-M Wolf Perez, P Sormanni, J Habchi, M Vendruscolo
– Nature reviews. Chemistry
(2021)
5,
277
The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition.
WK Man, B Tahirbegi, MD Vrettas, S Preet, L Ying, M Vendruscolo, A De Simone, G Fusco
– Nature communications
(2021)
12,
927
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk