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Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

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

Generic interactions in the condensed state of proteins
M Fuxreiter, M Vendruscolo
– EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2021)
50,
90
(link to publication)
Environmental Dependence of the Structure of the C-terminal Domain of the SARS-CoV-2 Envelope Protein
K Gadhave, A Kumar, P Kumar, S Kapuganti, N Garg, M Vendruscolo, R Giri
(2020)
2020.12.29.424646
(doi: 10.1101/2020.12.29.424646)
A method of incorporating rate constants as kinetic constraints in molecular dynamics simulations.
ZF Brotzakis, M Vendruscolo, PG Bolhuis
– Proceedings of the National Academy of Sciences of the United States of America
(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
– Biochim Biophys Acta Biomembr
(2020)
1863,
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
– Commun Chem
(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
– Proc Natl Acad Sci U S A
(2020)
117,
33254
(doi: 10.1073/pnas.2007670117)
Sequence determinants of the aggregation of proteins within condensates generated by liquid-liquid phase separation
M Vendruscolo, M Fuxreiter
(2020)
2020.12.07.414409
(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)
28,
70
(doi: 10.1016/j.chembiol.2020.11.002)
Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers.
RP Kreiser, AK Wright, NR Block, JE Hollows, LT Nguyen, K LeForte, B Mannini, M Vendruscolo, R Limbocker
– Int J Mol Sci
(2020)
21,
E8651
(doi: 10.3390/ijms21228651)
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
– biorxiv
(2020)
2020.11.10.376285
(doi: 10.1101/2020.11.10.376285)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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