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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

Erratum to: The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation (Scientific Reports, (2017), 7, 1, (9039), 10.1038/s41598-017-08324-z)
FA Aprile, E Källstig, G Limorenko, M Vendruscolo, D Ron, C Hansen
– Scientific reports
(2018)
8,
11848
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 (Cambridge, England)
(2018)
54,
8637
Stabilization and Characterization of Cytotoxic Aβ40 Oligomers Isolated from an Aggregation Reaction in the Presence of Zinc Ions.
B Mannini, J Habchi, S Chia, FS Ruggeri, M Perni, TPJ Knowles, CM Dobson, M Vendruscolo
– ACS Chemical Neuroscience
(2018)
Structural Ensemble Modulation upon Small-Molecule Binding to Disordered Proteins.
GT Heller, M Bonomi, M Vendruscolo
– Journal of molecular biology
(2018)
430,
2288
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
– J Neurosci Methods
(2018)
306,
57
Determination of the conformational states of strychnine in solution using NMR residual dipolar couplings in a tensor-free approach.
G Tomba, C Camilloni, M Vendruscolo
– Methods
(2018)
Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine.
M Perni, P Flagmeier, R Limbocker, R Cascella, FA Aprile, C Galvagnion, GT Heller, G Meisl, SW Chen, JR Kumita, PK Challa, JB Kirkegaard, SIA Cohen, B Mannini, D Barbut, EAA Nollen, C Cecchi, N Cremades, TPJ Knowles, F Chiti, M Zasloff, M Vendruscolo, CM Dobson
– ACS Chem Biol
(2018)
Reversible inhibition of the ClpP protease via an N-terminal conformational switch
S Vahidi, ZA Ripstein, M Bonomi, T Yuwen, MF Mabanglo, JB Juravsky, K Rizzolo, A Velyvis, WA Houry, M Vendruscolo, JL Rubinstein, LE Kay
– Proceedings of the National Academy of Sciences of the United States of America
(2018)
115,
E6447
Cooperative Assembly of Hsp70 Subdomain Clusters
MA Wright, FA Aprile, MMJ Bellaiche, TCT Michaels, T Müller, P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles
– Biochemistry
(2018)
57,
3641
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
(2018)
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk