ABETAALPHASYNTAU

"Insight into the synergistic interactions between Aβ amyloid, α-synuclein and Tau"

Coordinatore	BEN-GURION UNIVERSITY OF THE NEGEV    more  Organization address address: Office of the President - Main Campus city: BEER SHEVA postcode: 84105 contact info Titolo: Ms. Nome: Daphna Cognome: Tripto Email: send email Telefono: +972 8 6472435 Fax: +972 8 6472930
Nazionalità Coordinatore	Israel [IL]
Totale costo	100˙000 €
EC contributo	100˙000 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-2011-CIG
Funding Scheme	MC-CIG
Anno di inizio	2012
Periodo (anno-mese-giorno)	2012-03-01   -   2016-02-29

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	BEN-GURION UNIVERSITY OF THE NEGEV  Organization address address: Office of the President - Main Campus city: BEER SHEVA postcode: 84105 contact info Titolo: Ms. Nome: Daphna Cognome: Tripto Email: send email Telefono: +972 8 6472435 Fax: +972 8 6472930	IL (BEER SHEVA)	coordinator	100˙000.00

Mappa

 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

 Obiettivo del progetto (Objective)

'Protein aggregation is associated with numerous incurable diseases, including Aβ and tau proteins in Alzheimer’s disease (AD) and α-synuclein in Parkinson’s disease (PD). In vivo studies illustrate that these proteins appear in the brains of both AD and PD patients and that there are synergistic interactions between α-synuclein and tau, Aβ and tau, and α-synuclein and Aβ. Despite the accumulating in vivo evidence of the synergistic interactions between α-synuclein and tau, Aβ and tau, and α-synuclein and Aβ, the mechanism through which the protein pairs aggregate remains controversial. How and which interactions between two types of protein could be involved in protein aggregation is not completely understood. Moreover, it is still not clear which domains in these proteins can interact and what effects result from these interactions. To understand the mechanism of the aggregation between two types of protein, it is necessary to probe and characterize the molecular interactions between oligomers of these proteins. The challenge and the focus of this proposal are to identify the specific interactions between these protein pairs and to probe the oligomeric structures of the proteins at the molecular level. This proposal relies basically on computational tools (molecular modeling and molecular dynamics simulations). The modeling procedure will be based on experiemntal data (ssNMR, cryo-EM) and the constructed oligomeric structures will be validated by collaborative experimental work. The output of this project will be a detailed description of the interactions between proteins that are related to neurodegenerative diseases. Moreover, this proposal may provide insight into the link between AD and PD, and will pave the way to the development of potential drugs to alleviate/prevent the symptoms of neurodegenerative diseases by impending/preventing the interaction between the proteins.'