MAMBA

Molecular mechanism of amyloid β aggregation

 Coordinatore LUNDS UNIVERSITET 

Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.

 Nazionalità Coordinatore Sweden [SE]
 Totale costo 2˙499˙920 €
 EC contributo 2˙499˙920 €
 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-2013-ADG
 Funding Scheme ERC-AG
 Anno di inizio 2014
 Periodo (anno-mese-giorno) 2014-02-01   -   2019-01-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    LUNDS UNIVERSITET

 Organization address address: Paradisgatan 5c
city: LUND
postcode: 22100

contact info
Titolo: Mr.
Nome: Sanel
Cognome: Peric
Email: send email
Telefono: +4646222 81 21

SE (LUND) hostInstitution 2˙499˙920.00
2    LUNDS UNIVERSITET

 Organization address address: Paradisgatan 5c
city: LUND
postcode: 22100

contact info
Titolo: Prof.
Nome: Sara Elisabet
Cognome: Snogerup Linse
Email: send email
Telefono: +46 46 2228246
Fax: +46 46 2224116

SE (LUND) hostInstitution 2˙499˙920.00

Mappa


 Word cloud

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

alzheimer    methodology    intrinsic    cell    disease    amyloid    coupled    microscopic    extrinsic    toxic    steps    peptide    generation    kinetic    molecular    aggregation    species    function    oligomers   

 Obiettivo del progetto (Objective)

'Generation of toxic oligomers during aggregation of amyloid beta peptide (Abeta42) into amyloid fibrils is a central event in Alzheimer disease. Understanding the aggregation process is therefore one important step towards therapy and diagnosis of the disease. We propose a physical chemistry approach with the goal of finding the molecular mechanisms behind the process in terms of the underlying microscopic steps and the molecular driving forces governing each step. We will use methodology developed recently in our laboratory yielding unprecedented reproducibility in the kinetic data. The methodology relies on optimization of every step from production and purification to isolation of highly pure monomeric peptide, and inertness and minimized area of all surfaces. We will use cell viability studies to detect toxic oligomeric species, and selective radio-labeling experiments to pinpoint the origin of those species. In order to obtain insight into the molecular determinants and the relative role of different kinds of intermolecular interactions for each microscopic step, we will study the concentration dependent aggregation kinetics as a function of extrinsic and intrinsic parameters. Extrinsic parameters include temperature, salt, pH, biological membranes, other proteins, and low and high Mw inhibitors. Intrinsic parameters include point mutations and sequence extension/truncation. We will perform detailed kinetic studies for each inhibitor to learn which step in the process is inhibited coupled to cell toxicity assays to learn whether the generation of toxic oligomers is limited. We will use spectroscopic techniques, dynamic light scattering, cryogenic transmission electron microscopy and mass spectrometry coupled to HD exchange to learn about structural transitions as a function of process progression under different conditions to favor different microscopic steps. The results may lead to improved diagnostics and therapeutics of Alzheimer disease.'

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