SINGLEMOLALZHEIMER

Dissecting Alzheimer’s disease at a single molecule level

Coordinatore	LABORATORIO EUROPEO DI SPETTROSCOPIE NON LINEARI    more  Organization address address: Via Nello Carrara 1 city: Sesto-Fiorentino (FI) postcode: 50019 contact info Titolo: Prof. Nome: Francesco Cognome: Pavone Email: send email Telefono: 390555000000 Fax: 390555000000
Nazionalità Coordinatore	Italy [IT]
Totale costo	164˙458 €
EC contributo	164˙458 €
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-2009-IEF
Funding Scheme	MC-IEF
Anno di inizio	2011
Periodo (anno-mese-giorno)	2011-01-01   -   2013-12-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	LABORATORIO EUROPEO DI SPETTROSCOPIE NON LINEARI  Organization address address: Via Nello Carrara 1 city: Sesto-Fiorentino (FI) postcode: 50019 contact info Titolo: Prof. Nome: Francesco Cognome: Pavone Email: send email Telefono: 390555000000 Fax: 390555000000	IT (Sesto-Fiorentino (FI))	coordinator	164˙458.60

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 Obiettivo del progetto (Objective)

'Fibrillar deposits of proteins are the hallmark of amyloid diseases, amongst which Alzheimer’s disease stands out as the most widespread neurodegenerative pathology of the brain. Neuronal dysfunction is currently attributed to the interaction of A-beta oligomers with the plasma membrane. Several scenarios have been proposed, but the mechanisms of binding of the oligomers to the cell membrane and their subsequent toxicity is still unclear. The dependence of the proteolytic production of A-beta peptide on the distribution of the amyloid precursor protein (APP) and its proteases on the plasma membrane is also matter of debate.The discrepancies arising from the models proposed may be due to the fact that most of the current research on the molecular mechanisms of Alzheimer’s disease is based on averaged results obtained using bulk methods. In this case, many essential details can be missed. The goal of this project is to provide a better understanding of the pathogenesis of Alzheirmer’s disease by studying the dynamic features of this complex system at a single molecule level. In particular, the immediate aim will be to apply single molecule tracking techniques to characterize the mobility of A-beta oligomers on the plasmamembrane of living neuronal cells, especially with respect to synaptic structures and membrane rafts. In addition, I will study the surface mobility of the transmembrane proteins involved in A-beta production, namely APP, alpha-, beta-, and gamma-secretase. In the light of the influence of cholesterol on A-beta generation, my aim will be to study the dynamic response of these proteins to changes in cell cholesterol levels, and their location inside or outside lipid rafts. Overall, this project represents an innovative approach to understand the basic mechanisms underlying the development of Alzheirmer’s disease and to suggest new strategies for the cure of this pathological condition.'