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

Unraveling the Physicochemical Determinants of Protein Liquid-liquid Phase Separation by Nanoscale Infrared Vibrational Spectroscopy
FS Ruggeri, AM Miller, M Vendruscolo, TPJ Knowles
Bio Protocol
(2021)
11
Sequence Determinants of the Aggregation of Proteins Within Condensates Generated by Liquid-liquid Phase Separation
M Vendruscolo, M Fuxreiter
Journal of molecular biology
(2021)
434
Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine
S Errico, H Ramshini, C Capitini, C Canale, M Spaziano, D Barbut, M Calamai, M Zasloff, R Oropesa-Nuñez, M Vendruscolo, F Chiti
ACS chemical neuroscience
(2021)
12
Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins
U Nowicka, P Chroscicki, K Stroobants, M Sladowska, M Turek, B Uszczynska-Ratajczak, R Kundra, T Goral, M Perni, CM Dobson, M Vendruscolo, A Chacinska
eLife
(2021)
10
Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications.
R Bell, M Vendruscolo
Front Neurol
(2021)
12
Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
M Perni, B Mannini, CK Xu, JR Kumita, CM Dobson, F Chiti, M Vendruscolo
Scientific Reports
(2021)
11
Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response
P Joshi, M Perni, R Limbocker, B Mannini, S Casford, S Chia, J Habchi, J Labbadia, CM Dobson, M Vendruscolo
Commun Biol
(2021)
4
Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer's disease
DI Sideris, JSH Danial, D Emin, FS Ruggeri, Z Xia, YP Zhang, E Lobanova, H Dakin, S De, A Miller, JC Sang, TPJ Knowles, M Vendruscolo, G Fraser, D Crowther, D Klenerman
Brain communications
(2021)
3
Distinct responses of human peripheral blood cells to different misfolded protein oligomers
M Leal-Lasarte, B Mannini, F Chiti, M Vendruscolo, CM Dobson, C Roodveldt, D Pozo
Immunology
(2021)
164
Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers.
R Limbocker, R Staats, S Chia, FS Ruggeri, B Mannini, CK Xu, M Perni, R Cascella, A Bigi, LR Sasser, NR Block, AK Wright, RP Kreiser, ET Custy, G Meisl, S Errico, J Habchi, P Flagmeier, T Kartanas, JE Hollows, LT Nguyen, K LeForte, D Barbut, JR Kumita, C Cecchi, M Zasloff, TPJ Knowles, CM Dobson, F Chiti, M Vendruscolo
Front Neurosci
(2021)
15

Research Interest Groups

Telephone number

01223 763873

Email address