Structural studies of the interaction between Hsp70 and alpha-synuclein

Project Information

HSP70ASYN

Grant agreement ID: 275182

Project closed

Start date 1 August 2011

End date 31 July 2013

Funded under

• Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)

Total cost € 209 592,80

EU contribution € 209 592,80

Coordinated by

THE CHANCELLOR MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE
United Kingdom

Objective

"Protein misfolding and aggregation are associated with a wide range of severe, and so far incurable, neurological and systemic disorders, which include Alzheimer's and Parkinson's diseases, and type II diabetes. As these conditions are the consequence of the impairment of protein homeostasis, a variety of cellular natural defenses have evolved to eliminate protein aggregates as they form. In this application we are concerned with the problem of understanding the molecular basis of such defense mechanisms, by focusing on the specific case of the interaction between alpha-synuclein, a protein closely involved in Parkinson's disease, and Hsp70, a molecular chaperone with a variety of cellular functions, including the ability of recognising misfolded or aggregated proteins. We are going to address this problem using a wide arsenal of biophysical, biochemical and computational methods, including FRET and NMR spectroscopy, fluorescence methods, dynamic light scattering, transmission electron microscopy, isothermal titration calorimetry and molecular dynamics simulations. The outcome of this study will provide relevant structural information at atomic level on the binding modes of Hsp70 with diverse molecular forms of alpha-synuclein related to neurotoxicity. The results of this project are expected to increase our understanding of the molecular basis of the interactions between molecular chaperones and unstructured states of proteins, as well as to provide insights for the development of novel strategies for the rational design of therapeutic approaches against protein aggregation."

Fields of science

• natural sciences › physical sciences › optics › microscopy › electron microscopy
• natural sciences › computer and information sciences › computational science
• natural sciences › physical sciences › optics › spectroscopy › absorption spectroscopy
• natural sciences › biological sciences › biochemistry › biomolecules › proteins › protein folding
• natural sciences › chemical sciences › analytical chemistry › calorimetry

Programme(s)

• FP7-PEOPLE - Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)

Topic(s)

• FP7-PEOPLE-2010-IEF - Marie-Curie Action: "Intra-European fellowships for career development"

Call for proposal

FP7-PEOPLE-2010-IEF
See other projects for this call

Funding Scheme

MC-IEF - Intra-European Fellowships (IEF)

Coordinator

THE CHANCELLOR MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE

• EU contribution: € 209 592,80
• Address: TRINITY LANE THE OLD SCHOOLS ; CB2 1TN Cambridge ; United Kingdom
• Region: East of England › East Anglia › Cambridgeshire CC
• Activity type: Higher or Secondary Education Establishments
• Administrative Contact: Renata Schaeffer (Ms.)
• Total cost: No data