skip to content

Department of Chemistry

 
Portrait of mv245

 

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

Assessing motor-related phenotypes of Caenorhabditis elegans with the wide field-of-view nematode tracking platform.
M Koopman, Q Peter, RI Seinstra, M Perni, M Vendruscolo, CM Dobson, TPJ Knowles, EAA Nollen
– Nature protocols
(2020)
15,
2071
A kinetic ensemble of the Alzheimer’s Aβ peptide
T Löhr, K Kohlhoff, G Heller, C Camilloni, M Vendruscolo
(2020)
Complexity in Lipid Membrane Composition Induces Resilience to Aβ42 Aggregation
M Sanguanini, KN Baumann, S Preet, S Chia, J Habchi, TPJ Knowles, M Vendruscolo
– ACS chemical neuroscience
(2020)
11,
1347
Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.
TCT Michaels, A Šarić, S Curk, K Bernfur, P Arosio, G Meisl, AJ Dear, SIA Cohen, CM Dobson, M Vendruscolo, S Linse, TPJ Knowles
– Nature Chemistry
(2020)
12,
445
Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.
TCT Michaels, A Šarić, S Curk, K Bernfur, P Arosio, G Meisl, AJ Dear, SIA Cohen, CM Dobson, M Vendruscolo, S Linse, TPJ Knowles
– Nat Chem
(2020)
12,
497
A cell and tissue specific weakness of the protein homeostasis system underlies brain vulnerability to protein aggregation
R Kundra, CM Dobson, M Vendruscolo
– iScience
(2020)
23,
100934
Sequence-based determinants and prediction of fuzzy interactions in protein complexes
M Miskei, A Horvath, M Vendruscolo, M Fuxreiter
– Journal of molecular biology
(2020)
432,
2289
A single ultrasensitive assay for detection and discrimination of tau aggregates of Alzheimer and Pick diseases
MA Metrick, NDC Ferreira, E Saijo, A Kraus, K Newell, G Zanusso, M Vendruscolo, B Ghetti, B Caughey
– Acta Neuropathol Commun
(2020)
8,
22
Rational Design of Conformation-Specific Antibodies for Tau Oligomers
K Kulenkampff, FA Aprile, P Sormanni, RT Ranasinghe, D Klenerman, M Vendruscolo
– BIOPHYSICAL JOURNAL
(2020)
118,
370A
Polyglutamine Aggregation in a Living Animal is Governed by Biophysical Parameters
T Sinnige, T Michaels, M Vendruscolo, RI Morimoto
– BIOPHYSICAL JOURNAL
(2020)
118,
372A
  • <
  • 2 of 57
  • >

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk