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

Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
R Limbocker, S Chia, FS Ruggeri, M Perni, R Cascella, GT Heller, G Meisl, B Mannini, J Habchi, TCT Michaels, PK Challa, M Ahn, ST Casford, N Fernando, CK Xu, ND Kloss, SIA Cohen, JR Kumita, C Cecchi, M Zasloff, S Linse, TPJ Knowles, F Chiti, M Vendruscolo, CM Dobson
– Nature Communications
(2019)
10,
225
Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's β-amyloid aggregation.
M Ahn, BI Lee, S Chia, J Habchi, JR Kumita, M Vendruscolo, CM Dobson, CB Park
– Chemical communications (Cambridge, England)
(2019)
A tau homeostasis signature is linked with the cellular and regional vulnerability of excitatory neurons to tau pathology
H Fu, A Possenti, R Freer, Y Nakano, NCH Villegas, M Tang, PVM Cauhy, BA Lassus, S Chen, SL Fowler, HY Figueroa, ED Huey, GVW Johnson, M Vendruscolo, KE Duff
– Nature Neuroscience
(2019)
22,
47
A superposition free method for protein conformational ensemble analyses and local clustering based on a differential geometry representation of backbone
A Marinho da Silva Neto, SR Silva, M Vendruscolo, C Camilloni, RW Montalvao
– Proteins
(2018)
In vitro and in silico assessment of the developability of a designed monoclonal antibody library.
A-M Wolf Pérez, P Sormanni, JS Andersen, LI Sakhnini, I Rodriguez-Leon, JR Bjelke, AJ Gajhede, L De Maria, DE Otzen, M Vendruscolo, N Lorenzen
– MAbs
(2018)
19420862.2018.1556082
Determination of protein structural ensembles using cryo-electron microscopy
M Bonomi, M Vendruscolo
– Current opinion in structural biology
(2018)
56,
37
Determination of Structural Ensembles of Proteins: Restraining vs Reweighting.
R Rangan, M Bonomi, GT Heller, A Cesari, G Bussi, M Vendruscolo
– Journal of Chemical Theory and Computation
(2018)
14,
6632
Automated Behavioral Analysis of Large C. elegans Populations Using a Wide Field-of-view Tracking Platform.
M Perni, S Casford, FA Aprile, EA Nollen, TPJ Knowles, M Vendruscolo, CM Dobson
– Journal of visualized experiments : JoVE
(2018)
2018,
(DOI: 10.3791/58643)
Third generation antibody discovery methods: in silico rational design
P Sormanni, FA Aprile, M Vendruscolo
– Chemical Society Reviews
(2018)
47,
9137
A bioinformatics approach to define the aggregation capacity of the myofiber proteome in inclusion body myositis
C Weihl, P Ciryam, A Guttsches, K Marcus, R Morimoto, M Vendruscolo, R Kley
– Neuromuscular Disorders
(2018)
28,
S77
  • 1 of 49
  • >

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk