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Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

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 Caenorhabditis elegans
C Huang, S Wagner-Valladolid, AD Stephens, R Jung, C Poudel, T Sinnige, MC Lechler, N Schlörit, M Lu, RF Laine, CH Michel, M Vendruscolo, CF Kaminski, GS Kaminski Schierle, DC David
– Elife
(2019)
8,
e43059
(doi: 10.7554/elife.43059)
Identifying A- and P-site locations on ribosome-protected mRNA fragments using Integer Programming.
N Ahmed, P Sormanni, P Ciryam, M Vendruscolo, CM Dobson, EP O'Brien
– Sci Rep
(2019)
9,
6256
(doi: 10.1038/s41598-019-42348-x)
Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-β aggregates
T Scheidt, U Łapińska, JR Kumita, DR Whiten, D Klenerman, MR Wilson, SIA Cohen, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles, P Arosio
– Science Advances
(2019)
5,
eaau3112
(doi: 10.1126/sciadv.aau3112)
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
– Scientific reports
(2019)
9,
5822
(doi: 10.1038/s41598-019-41925-4)
ADSoluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer’s disease progression
S De, D Whiten, F Ruggeri, C Hughes, M Rodrigues, D Sideris, C Taylor, F Aprile, S Muyldermans, T Knowles, M Vendruscolo, C Bryant, K Blennow, I Skoog, S Kern, H Zetterberg, D Klenerman
(2019)
600346
(doi: 10.1101/600346)
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms.
S De, DC Wirthensohn, P Flagmeier, C Hughes, FA Aprile, FS Ruggeri, DR Whiten, D Emin, Z Xia, JA Varela, P Sormanni, F Kundel, TPJ Knowles, CM Dobson, C Bryant, M Vendruscolo, D Klenerman
– Nature Communications
(2019)
10,
1541
(doi: 10.1038/s41467-019-09477-3)
The metastability of the proteome of spinal motor neurons underlies their selective vulnerability in ALS.
JJ Yerbury, L Ooi, IP Blair, P Ciryam, CM Dobson, M Vendruscolo
– Neurosci Lett
(2019)
704,
89
(doi: 10.1016/j.neulet.2019.04.001)
A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli.
K Sanagavarapu, E Nüske, I Nasir, G Meisl, JN Immink, P Sormanni, M Vendruscolo, TPJ Knowles, A Malmendal, C Cabaleiro-Lago, S Linse
– Scientific reports
(2019)
9,
3680
(doi: 10.1038/s41598-019-39216-z)
Atomic force microscopy for single molecule characterisation of protein aggregation
FS Ruggeri, T Šneideris, M Vendruscolo, TPJ Knowles
– Archives of biochemistry and biophysics
(2019)
664,
134
(doi: 10.1016/j.abb.2019.02.001)
A superposition free method for protein conformational ensemble analyses and local clustering based on a differential geometry representation of backbone.
AM da Silva Neto, SR Silva, M Vendruscolo, C Camilloni, RW Montalvão
– Proteins: Structure, Function and Bioinformatics
(2019)
87,
302
(doi: 10.1002/prot.25652)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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