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

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
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
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
Single amyloid aggregates chemical and structural analysis by infrared nanospectroscopy
FS Ruggeri, J Habchi, C Sean, M Vendruscolo, TPJ Knowles
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
Structural characterisation of the early events in the nucleation-condensation mechanism of folding
P Kukic, Y Pustovalova, C Camilloni, S Gianni, DM Korzhnev, M Vendruscolo
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
Mechanisms of Amyloid-β 42 oligomer formation from kinetic analysis
TC Michaels, A Saric, HW Lazell, P Arosio, M Vendruscolo, CM Dobson, S Linse, TPJ Knowles
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
46
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
Selective targeting of primary and secondary nucleation pathways in Aβ42 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
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
Structural basis of synaptic vesicle assembly promoted by α-synuclein (vol 7, 12563, 2016)
G Fusco, T Pape, AD Stephens, P Mahou, AR Costa, CF Kaminski, GSK Schierle, M Vendruscolo, G Veglia, CM Dobson, A De Simone
Nature communications
(2017)
8

Research Interest Groups

Telephone number

01223 763873

Email address