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

Characterization of the conformational fluctuations in the Josephin domain of ataxin-3.
D Sanfelice, A De Simone, A Cavalli, S Faggiano, M Vendruscolo, A Pastore
Biophysical Journal
(2014)
107
The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein
R Porcari, C Proukakis, CA Waudby, B Bolognesi, PP Mangione, JFS Paton, S Mullin, LD Cabrita, A Penco, A Relini, G Verona, M Vendruscolo, M Stoppini, GG Tartaglia, C Camilloni, J Christodoulou, AHV Schapira, V Bellotti
J Biol Chem
(2014)
290
ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load.
JE Chambers, K Petrova, G Tomba, M Vendruscolo, D Ron
J Cell Biol
(2014)
207
ADP ribosylation adapts an ER chaperone response to short-term fluctuations in unfolded protein load
JE Chambers, K Petrova, G Tomba, M Vendruscolo, D Ron
The Journal of cell biology
(2014)
207
A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein.
JR Allison, RC Rivers, JC Christodoulou, M Vendruscolo, CM Dobson
Biochemistry
(2014)
53
The CamSol method of rational design of protein mutants with enhanced solubility.
P Sormanni, FA Aprile, M Vendruscolo
Journal of molecular biology
(2014)
427
Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein.
S Gianni, C Camilloni, R Giri, A Toto, D Bonetti, A Morrone, P Sormanni, M Brunori, M Vendruscolo
Proc Natl Acad Sci U S A
(2014)
111
Identification and characterization of PKCγ, a kinase associated with SCA14, as an amyloidogenic protein
H Takahashi, N Adachi, T Shirafuji, S Danno, T Ueyama, M Vendruscolo, AN Shuvaev, T Sugimoto, T Seki, D Hamada, K Irie, H Hirai, N Sakai, N Saito
Human Molecular Genetics
(2014)
24
Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts.
W Boomsma, P Tian, J Frellsen, J Ferkinghoff-Borg, T Hamelryck, K Lindorff-Larsen, M Vendruscolo
Proceedings of the National Academy of Sciences
(2014)
111
NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain.
HTA Leung, P Kukic, C Camilloni, F Bemporad, A De Simone, FA Aprile, JR Kumita, M Vendruscolo
Protein Science
(2014)
23

Research Interest Groups

Telephone number

01223 763873

Email address