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

Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans
C Huang, S Wagner-Valladolid, AD Stephens, R Jung, C Poudel, T Sinnige, MC Lechler, N Schlörit, RF Laine, CH Michel, M Vendruscolo, CF Kaminski, GSK Schierle, DC David
(2018)
Fast fluorescence lifetime imaging reveals the aggregation processes of α-synuclein and polyglutamine in aging Caenorhabditis elegans
RF Laine, T Sinnige, K Yu, AJ Haack, C Poudel, P Gaida, N Curry, M Perni, EAA Nollen, CM Dobson, M Vendruscolo, GSK Schierle, CF Kaminski
(2018)
Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis.
CA Waudby, T Wlodarski, M-E Karyadi, AME Cassaignau, SHS Chan, AS Wentink, JM Schmidt-Engler, C Camilloni, M Vendruscolo, LD Cabrita, J Christodoulou
Proceedings of the National Academy of Sciences
(2018)
115
A method for partitioning the information contained in a protein sequence between its structure and function
A Possenti, M Vendruscolo, C Camilloni, G Tiana
Proteins: Structure, Function, and Bioinformatics
(2018)
86
A structural ensemble modulation mechanism of small molecule binding to disordered proteins
GT Heller, M Bonomi, M Vendruscolo
J Mol Biol
(2018)
430
Massively parallel C. elegans tracking provides multi-dimensional fingerprints for phenotypic discovery.
M Perni, PK Challa, JB Kirkegaard, R Limbocker, M Koopman, MC Hardenberg, P Sormanni, T Müller, KL Saar, LWY Roode, J Habchi, G Vecchi, N Fernando, S Casford, EAA Nollen, M Vendruscolo, CM Dobson, TPJ Knowles
Journal of neuroscience methods
(2018)
306
Structural differences between toxic and nontoxic HypF-N oligomers
C Capitini, JR Patel, A Natalello, C D'Andrea, A Relini, JA Jarvis, L Birolo, A Peduzzo, M Vendruscolo, P Matteini, CM Dobson, A De Simone, F Chiti
Chemical Communications
(2018)
54
Molecular dynamics ensemble refinement of the heterogeneous native state of NCBD using chemical shifts and NOEs.
E Papaleo, C Camilloni, K Teilum, M Vendruscolo, K Lindorff-Larsen
PeerJ
(2018)
2018
Exploring the role of post-translational modifications in regulating -synuclein interactions by studying the effects of phosphorylation on nanobody binding
F El Turk, E De Genst, T Guilliams, B Fauvet, M Hejjaoui, J Di Trani, A Chiki, A Mittermaier, M Vendruscolo, HA Lashuel, CM Dobson
Protein Science
(2018)
27
O2‐02‐02: TARGETING AMYLOID FORMATION USING RATIONALLY DESIGNED ANTIBODIES
FA Aprile, P Sormanni, M Perni, P Arosio, R Limbocker, S Chhangur, B Mannini, S Linse, T Knowles, CM Dobson, M Vendruscolo
Alzheimer's & Dementia
(2018)
14

Research Interest Groups

Telephone number

01223 763873

Email address