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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

Proteome folding and aggregation

M Vendruscolo

– Current opinion in structural biology

(2012)

22,

138

(doi: 10.1016/j.sbi.2012.01.005)

Fibrillogenic propensity of the GroEL apical domain

J Chen, H Yagi, P Sormanni, M Vendruscolo, K Makabe, T Nakamura, Y Goto, K Kuwajima

– PROTEIN SCIENCE

(2012)

21,

102

(link to publication)

NMR chemical shifts and protein dynamics

C Camilloni, M Vendruscolo

– FEBS JOURNAL

(2012)

279,

529

(link to publication)

Anti-oligomer monoclonal antibodies reveal that protein aggregation modulates generalized physiological and pathological disturbances

M Tayebi, M Vendruscolo, M David

– PRION

(2012)

6,

77

(link to publication)

Co-translational folding of E. coli's cytosolic proteome exhibits kinetic effects that can significantly delay folding

P Ciryam, M Vendruscolo, CM Dobson, EP O'Brien

– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY

(2012)

244,

(link to publication)

Protein Structure Validation Using Side-Chain Chemical Shifts

AB Sahakyan, A Cavalli, WF Vranken, M Vendruscolo

– The Journal of Physical Chemistry B

(2012)

116,

4754

(doi: 10.1021/jp2122054)

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

A De Simone, A Dhulesia, G Soldi, M Vendruscolo, S-TD Hsu, F Chiti, CM Dobson

– Proc Natl Acad Sci U S A

(2011)

108,

21057

(doi: 10.1073/pnas.1112197108)

Sequence-Based Prediction of Protein Solubility

F Agostini, M Vendruscolo, GG Tartaglia

– Journal of molecular biology

(2011)

421,

237

(doi: 10.1016/j.jmb.2011.12.005)

Protein solubility and protein homeostasis: A generic view of protein misfolding disorders

M Vendruscolo, TPJ Knowles, CM Dobson

– Cold Spring Harbor Perspectives in Biology

(2011)

3,

(doi: 10.1101/cshperspect.a010454)

Coarse-grained model for protein folding based on structural profiles

K Wolff, M Vendruscolo, M Porto

– Physical Review E - Statistical, Nonlinear, and Soft Matter Physics

(2011)

84,

041934

(doi: 10.1103/physreve.84.041934)