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Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

Portrait of mv245

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

Facile Installation of Post-translational Modifications on the Tau Protein via Chemical Mutagenesis.
PR Lindstedt, RJ Taylor, GJL Bernardes, M Vendruscolo
– ACS chemical neuroscience
(2021)
acschemneuro.0c00761
(DOI: 10.1021/acschemneuro.0c00761)
A kinetic ensemble of the Alzheimer’s Aβ peptide
T Löhr, K Kohlhoff, GT Heller, C Camilloni, M Vendruscolo
– Nature Computational Science
(2021)
1,
71
(DOI: 10.1038/s43588-020-00003-w)
A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
R Cataldi, S Chia, K Pisani, FS Ruggeri, CK Xu, T Šneideris, M Perni, S Sarwat, P Joshi, JR Kumita, S Linse, J Habchi, TPJ Knowles, B Mannini, CM Dobson, M Vendruscolo
– Communications biology
(2021)
4,
19
(DOI: 10.1038/s42003-020-01490-3)
Observation of an α-1synuclein liquid droplet state and its maturation into Lewy body-like assemblies
MC Hardenberg, T Sinnige, S Casford, S Dada, C Poudel, EA Robinson, M Fuxreiter, C Kaminksi, GS Kaminski-Schierle, EAA Nollen, CM Dobson, M Vendruscolo
– Journal of molecular cell biology
(2021)
mjaa075-
(DOI: 10.1093/jmcb/mjaa075)
A method of incorporating rate constants as kinetic constraints in molecular dynamics simulations
ZF Brotzakis, M Vendruscolo, PG Bolhuis
– Proc Natl Acad Sci U S A
(2020)
118,
e2012423118
(DOI: 10.1073/pnas.2012423118)
Interactions of α-synuclein oligomers with lipid membranes.
G Musteikytė, AK Jayaram, CK Xu, M Vendruscolo, G Krainer, TPJ Knowles
– Biochimica et biophysica acta. Biomembranes
(2020)
183536
(DOI: 10.1016/j.bbamem.2020.183536)
Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter
R Staats, TCT Michaels, P Flagmeier, S Chia, RI Horne, J Habchi, S Linse, TPJ Knowles, CM Dobson, M Vendruscolo
– Communications Chemistry
(2020)
3,
191
(DOI: 10.1038/s42004-020-00412-y)
Widespread occurrence of the droplet state of proteins in the human proteome
M Hardenberg, A Horvath, V Ambrus, M Fuxreiter, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2020)
117,
33254
(DOI: 10.1073/pnas.2007670117)
Sequence determinants for the aggregation and cytotoxicity of proteins within condensates generated by liquid-liquid phase separation
M Vendruscolo, M Fuxreiter
(2020)
(DOI: 10.1101/2020.12.07.414409)
Systematic Activity Maturation of a Single-Domain Antibody with Non-canonical Amino Acids through Chemical Mutagenesis
PR Lindstedt, FA Aprile, P Sormanni, R Rakoto, CM Dobson, GJL Bernardes, M Vendruscolo
– Cell chemical biology
(2020)
(DOI: 10.1016/j.chembiol.2020.11.002)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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