skip to content
Home

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

Scaling behaviour and rate-determining steps in filamentous self-assembly
G Meisl, L Rajah, SAI Cohen, M Pfammatter, A Šarić, E Hellstrand, AK Buell, A Aguzzi, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles
– Chemical Science
(2017)
8,
7087
(doi: 10.1039/c7sc01965c)
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation.
F aprile, E Källstig, G Limorenko, Vendruscolo, D Ron, C hansen
– Scientific Reports
(2017)
7,
9039
(doi: 10.1038/s41598-017-08324-z)
Rapid and accurate in silico solubility screening of a monoclonal antibody library.
P Sormanni, L Amery, S Ekizoglou, M Vendruscolo, B Popovic
– Scientific reports
(2017)
7,
8200
(doi: 10.1038/s41598-017-07800-w)
Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates
S Chia, P Flagmeier, J Habchi, V Lattanzi, S Linse, CM Dobson, TPJ Knowles, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2017)
114,
8005
(doi: 10.1073/pnas.1700239114)
Protein homeostasis of a metastable subproteome associated with Alzheimer's disease
R Kundra, P Ciryam, RI Morimoto, CM Dobson, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
114,
E5703
(doi: 10.1073/pnas.1618417114)
Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species
D Klenerman, M Iljina, L Hong, MH Horrocks, MH Ludtmann, ML Choi, CD Hughes, FS Ruggeri, T Guilliams, AK Buell, J-E Lee, S Gandhi, SF Lee, CE Bryant, M Vendruscolo, TPJ Knowles, CM Dobson, E De Genst, D Klenerman
– BMC biology
(2017)
15,
57
(doi: 10.1186/s12915-017-0390-6)
Amyloid-like Fibrils from an α-Helical Transmembrane Protein.
K Stroobants, JR Kumita, NJ Harris, DY Chirgadze, CM Dobson, PJ Booth, M Vendruscolo
– Biochemistry
(2017)
56,
3225
(doi: 10.1021/acs.biochem.7b00157)
Protein homeostasis of a metastable subproteome associated with Alzheimer's disease.
R Kundra, P Ciryam, RI Morimoto, CM Dobson, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
114,
e5703
(doi: 10.1073/pnas.1618417114)
Selective targeting of primary and secondary nucleation pathways in Ab42 aggregation using a rational antibody scanning method
FA Aprile, P Sormanni, M Perni, P Arosio, S Linse, TPJ Knowles, CM Dobson, M Vendruscolo
– Science advances
(2017)
3,
e1700488
(doi: 10.1126/sciadv.1700488)
Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.
A Munke, J Persson, T Weiffert, E De Genst, G Meisl, P Arosio, A Carnerup, CM Dobson, M Vendruscolo, TPJ Knowles, S Linse
– Proc Natl Acad Sci U S A
(2017)
114,
6444
(doi: 10.1073/pnas.1700407114)
  • <
  • 36 of 80
  • >

Research Groups

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk

    Study at Cambridge

    About the University

    Research at Cambridge