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

Paratope Prediction using Convolutional and Recurrent Neural Networks
E Liberis, P Veličković, P Sormanni, M Vendruscolo, P Liò
(2017)
Sequence Specificity in the Entropy-Driven Binding of a Small Molecule and a Disordered Peptide
GT Heller, FA Aprile, M Bonomi, C Camilloni, A De Simone, M Vendruscolo
J Mol Biol
(2017)
429
Methods of probing the interactions between small molecules and disordered proteins
GT Heller, FA Aprile, M Vendruscolo
Cell Mol Life Sci
(2017)
74
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
Chem Sci
(2017)
8
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
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
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 of the United States of America
(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 Biol
(2017)
15
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

Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address