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Structural studies of the interaction between Hsp70 and alpha-synuclein

Project information

Grant agreement ID: 275182

Status

Closed project

  • Start date

    1 August 2011

  • End date

    31 July 2013

Funded under:

FP7-PEOPLE

  • Overall budget:

    € 209 592,80

  • EU contribution

    € 209 592,80

Coordinated by:

THE CHANCELLOR MASTERS AND SCHOLARSOF 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."

Coordinator

THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE

Address

Trinity Lane The Old Schools
Cb2 1tn Cambridge

United Kingdom

Activity type

Higher or Secondary Education Establishments

EU Contribution

€ 209 592,80

Administrative Contact

Renata Schaeffer (Ms.)

Project information

Grant agreement ID: 275182

Status

Closed project

  • Start date

    1 August 2011

  • End date

    31 July 2013

Funded under:

FP7-PEOPLE

  • Overall budget:

    € 209 592,80

  • EU contribution

    € 209 592,80

Coordinated by:

THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE

United Kingdom