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

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
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
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
Correction: Corrigendum: Structural basis of synaptic vesicle assembly promoted by α-synuclein
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
Structural Characterization of the Early Events in the Nucleation–Condensation Mechanism in a Protein Folding Process
P Kukic, Y Pustovalova, C Camilloni, S Gianni, DM Korzhnev, M Vendruscolo
J Am Chem Soc
(2017)
139
The RNF168 paralog RNF169 defines a new class of ubiquitylated histone reader involved in the response to DNA damage.
J Kitevski-LeBlanc, A Fradet-Turcotte, P Kukic, MD Wilson, G Portella, T Yuwen, S Panier, S Duan, MD Canny, H van Ingen, CH Arrowsmith, JL Rubinstein, M Vendruscolo, D Durocher, LE Kay
eLife
(2017)
6
Emergence and evolution of an interaction between intrinsically disordered proteins
G Hultqvist, E Åberg, C Camilloni, GN Sundell, E Andersson, J Dogan, CN Chi, M Vendruscolo, P Jemth
Elife
(2017)
6
Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS
P Ciryam, IA Lambert-Smith, DM Bean, R Freer, F Cid, GG Tartaglia, DN Saunders, MR Wilson, SG Oliver, RI Morimoto, CM Dobson, M Vendruscolo, G Favrin, JJ Yerbury
Proceedings of the National Academy of Sciences of USA
(2017)
114
MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.
Y Yoshimura, MA Holmberg, P Kukic, CB Andersen, A Mata-Cabana, SF Falsone, M Vendruscolo, EAA Nollen, FAA Mulder
The Journal of biological chemistry
(2017)
292
Simultaneous quantification of protein order and disorder
P Sormanni, D Piovesan, GT Heller, M Bonomi, P Kukic, C Camilloni, M Fuxreiter, Z Dosztanyi, RV Pappu, MM Babu, S Longhi, P Tompa, AK Dunker, VN Uversky, SCE Tosatto, M Vendruscolo
Nat Chem Biol
(2017)
13

Research Interest Groups

Telephone number

01223 763873

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