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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

Trodusquemine enhances Aβ
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
The free energy landscape of the oncogene protein E7 of human papillomavirus type 16 reveals a complex interplay between ordered and disordered regions.
P Kukic, GM Lo Piccolo, MO Nogueira, DI Svergun, M Vendruscolo, IC Felli, R Pierattelli
– Sci Rep
(2019)
9,
5822
Enhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational Modification.
PR Lindstedt, FA Aprile, MJ Matos, M Perni, JB Bertoldo, B Bernardim, Q Peter, G Jiménez-Osés, TPJ Knowles, CM Dobson, F Corzana, M Vendruscolo, GJL Bernardes
– ACS Central Science
(2019)
5,
1417
A Practical Guide to the Simultaneous Determination of Protein Structure and Dynamics Using Metainference
T Löhr, C Camilloni, M Bonomi, M Vendruscolo
– Methods in molecular biology (Clifton, N.J.)
(2019)
2022,
313
Small molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer’s disease
G Heller, F Aprile, T Michaels, R Limbocker, M Perni, FS Ruggeri, B Mannini, T Löhr, M Bonomi, A De Simone, I Felli, R Pierattelli, T Knowles, C Dobson, M Vendruscolo
(2019)
Promoting transparency and reproducibility in enhanced molecular simulations
PLUMED consortium
– Nature methods
(2019)
16,
670
The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli.
L Zhao, G Vecchi, M Vendruscolo, R Körner, M Hayer-Hartl, FU Hartl
– Cell Rep
(2019)
28,
1335
Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer’s disease progression
S De, DR Whiten, FS Ruggeri, C Hughes, M Rodrigues, DI Sideris, CG Taylor, FA Aprile, S Muyldermans, TPJ Knowles, M Vendruscolo, C Bryant, K Blennow, I Skoog, S Kern, H Zetterberg, D Klenerman
– Acta neuropathologica communications
(2019)
7,
120
Differential Interactome and Innate Immune Response Activation of Two Structurally Distinct Misfolded Protein Oligomers.
B Mannini, G Vecchi, A Labrador-Garrido, B Fabre, G Fani, JM Franco, K Lilley, D Pozo, M Vendruscolo, F Chiti, CM Dobson, C Roodveldt
– ACS Chemical Neuroscience
(2019)
10,
3464
Determination of protein structural ensembles using cryo-electron microscopy.
M Bonomi, M Vendruscolo
– Current Opinion in Structural Biology
(2019)
56,
37
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk