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

Chemical kinetics for drug discovery to combat protein aggregation diseases

P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles

– Trends in Pharmacological Sciences

(2014)

35,

127

(doi: 10.1016/j.tips.2013.12.005)

Chemical kinetics for drug discovery to combat protein aggregation diseases

P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles

– Trends in pharmacological sciences

(2014)

35,

127

(doi: 10.1016/j.tips.2013.12.005)

Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease

G Tóth, SJ Gardai, W Zago, CW Bertoncini, N Cremades, SL Roy, MA Tambe, J-C Rochet, C Galvagnion, G Skibinski, S Finkbeiner, M Bova, K Regnstrom, S-S Chiou, J Johnston, K Callaway, JP Anderson, MF Jobling, AK Buell, TA Yednock, TPJ Knowles, M Vendruscolo, J Christodoulou, CM Dobson, D Schenk, L McConlogue

– PloS one

(2014)

e87133

(doi: 10.1371/journal.pone.0087133)

The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide

AA Kendrick, MJ Holliday, NG Isern, F Zhang, C Camilloni, C Huynh, M Vendruscolo, G Armstrong, EZ Eisenmesser

– Protein science : a publication of the Protein Society

(2014)

23,

464

(doi: 10.1002/pro.2430)

Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.

P Kukic, C Camilloni, A Cavalli, M Vendruscolo

– Journal of molecular biology

(2014)

426,

1826

(doi: 10.1016/j.jmb.2014.02.002)

A Conformational Ensemble Derived Using NMR Methyl Chemical Shifts Reveals a Mechanical Clamping Transition That Gates the Binding of the HU Protein to DNA

A Kannan, C Camilloni, AB Sahakyan, A Cavalli, M Vendruscolo

– Journal of the American Chemical Society

(2014)

136,

2204

(doi: 10.1021/ja4105396)