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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

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.

SIA Cohen, P Arosio, J Presto, FR Kurudenkandy, H Biverstal, L Dolfe, C Dunning, X Yang, B Frohm, M Vendruscolo, J Johansson, CM Dobson, A Fisahn, TPJ Knowles, S Linse

– Nature Structural and Molecular Biology

(2015)

22,

207

(doi: 10.1038/nsmb.2971)

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

C Galvagnion, AK Buell, G Meisl, TCT Michaels, M Vendruscolo, TPJ Knowles, CM Dobson

– Nat Chem Biol

(2015)

11,

229

(doi: 10.1038/NCHEMBIO.1750)

The CamSol method of rational design of protein mutants with enhanced solubility

P Sormanni, FA Aprile, M Vendruscolo

– Journal of Molecular Biology

(2015)

427,

478

(doi: 10.1016/j.jmb.2014.09.026)

Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.

P Ciryam, R Kundra, RI Morimoto, CM Dobson, M Vendruscolo

– Trends in pharmacological sciences

(2015)

36,

72

(doi: 10.1016/j.tips.2014.12.004)

Analysis of the hierarchical structure of the B. subtilis transcriptional regulatory network

S Kumar, M Vendruscolo, A Singh, D Kumar, A Samal

– Mol Biosyst

(2015)

11,

930

(doi: 10.1039/c4mb00298a)

Structure of a low-population intermediate state in the release of an enzyme product

A De Simone, FA Aprile, A Dhulesia, CM Dobson, M Vendruscolo

– Elife

(2015)

4,

e02777

(doi: 10.7554/elife.02777)

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

C Galvagnion, AK Buell, G Meisl, TCT Michaels, M Vendruscolo, TPJ Knowles, CM Dobson

– Nature Chemical Biology

(2015)

11,

229

(doi: 10.1038/nchembio.1750)

The Computational Studies of Co-Translational Protein Folding

T Wlodarski, C Waudby, C Sammy, M Vendruscolo, J Christodoulou

– Biophysical Journal

(2015)

108,

515a

(doi: 10.1016/j.bpj.2014.11.2823)

Rapid sizing of proteins in complex solutions

P Arosio, T Muller, L Rajah, EV Yates, FA Aprile, SIA Cohen, DA White, TW Herling, E de Genst, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles

– EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS

(2015)

44,

S49

(link to publication)

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

C Galvagnion, AK Buell, G Meisl, TC Michaels, M Vendruscolo, TPJ Knowles, CM Dobson

– EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS

(2015)

44,

S101

(link to publication)