NOVEL TOOLS IN PD

Novel tools for real time monitoring and quantification of protein aggregation in Parkinson s disease and related neurodegenerative disorders

Coordinatore	ECOLE POLYTECHNIQUE FEDERALE DE LAUSANNE    more Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.
Nazionalità Coordinatore	Switzerland [CH]
Totale costo	1˙495˙400 €
EC contributo	1˙495˙400 €
Programma	FP7-IDEAS-ERC Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	ERC-2009-StG
Funding Scheme	ERC-SG
Anno di inizio	2009
Periodo (anno-mese-giorno)	2009-12-01   -   2014-11-30

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	ECOLE POLYTECHNIQUE FEDERALE DE LAUSANNE  Organization address address: BATIMENT CE 3316 STATION 1 city: LAUSANNE postcode: 1015 contact info Titolo: Ms. Nome: Caroline Cognome: Vandevyver Email: send email Telefono: +41 21 693 4977 Fax: +41 21 693 5585	CH (LAUSANNE)	hostInstitution	1˙495˙400.00
2	ECOLE POLYTECHNIQUE FEDERALE DE LAUSANNE  Organization address address: BATIMENT CE 3316 STATION 1 city: LAUSANNE postcode: 1015 contact info Titolo: Prof. Nome: Hilal Cognome: Lashuel Email: send email Telefono: -6939671 Fax: -6931760	CH (LAUSANNE)	hostInstitution	1˙495˙400.00

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 Obiettivo del progetto (Objective)

'To understand the molecular basis of any biological process, it is critical that one is not only able to visualize and monitor molecular events that underlie this process, but also to possess the tools to manipulate these events in a spatial and temporal fashion both in and out of the cell. The overall objective of this proposal is to apply chemical biology approaches to allow real time monitoring of protein aggregation and to dissect the role of specific disease-associated post-translational modifications, phosphorylation, nitration, and truncation on the structure, aggregation, and biochemical properties of monomeric a-syn in health and disease. To achieve these goals, we plan to use a combination of organic chemistry, molecular biology, proteomics, protein engineering, and semisynthetic strategies to facilitate site-specific introduction of post-translational modifications that can be masked and activated in a controllable manner, both inside and outside living cells. Modified synthetic ±-syn will be introduced into primary neurons and cellular models of synucleinopathies and the consequences of masking or activating specific modifications will be assessed using biochemical, immunofluorescence, and live imaging techniques (Specific Aim 1). The absence of specific molecular probes that allow in vivo monitoring and quantitative measurement of toxic misfolded and aggregation intermediates represents a major impediment to understanding the relationship among protein misfolding, post-translational modification, protein aggregation, neurodegeneration, and cell death in PD and other neurodegenerative disorders. To address this challenge, we plan to develop and characterize novel antibodies that target different species along the amyloid formation pathway of ±-syn (Specific Aim 2).'