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Centre for Misfolding Diseases

Professor Michele Vendruscolo

 

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.

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.

 

 

Publications

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
– Journal of molecular biology
(2017)
429,
2772
Methods of probing the interactions between small molecules and disordered proteins.
GT Heller, FA Aprile, M Vendruscolo
– Cellular and Molecular Life Sciences
(2017)
74,
3225
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress alpha-synuclein aggregation
FA Aprile, E Källstig, G Limorenko, M Vendruscolo, D Ron, C Hansen
– Scientific reports
(2017)
7,
9039
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
Monomeric and fibrillar alpha-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of A beta 42 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,
8005
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
Nanobodies raised against monomeric alpha-synuclein inhibit fibril formation and destabilize toxic oligomeric species
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
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
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
– Sci Adv
(2017)
3,
e1700488
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
– Proceedings of the National Academy of Sciences of the United States of America
(2017)
114,
6444
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Research Interest Groups

Telephone number

01223 763873

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