PROTEPROBE

Electrically Controlled Protein Conformation on 3D Tissue Scaffolds

 Coordinatore Ecole Nationale Supérieure des Mines de Saint-Etienne 

 Organization address address: COURS FAURIEL 158
city: SAINT ETIENNE CEDEX
postcode: 42023

contact info
Titolo: Mr.
Nome: Christophe
Cognome: Obidig
Email: send email
Telefono: 33442616613

 Nazionalità Coordinatore France [FR]
 Totale costo 269˙743 €
 EC contributo 269˙743 €
 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-2012-IEF
 Funding Scheme MC-IEF
 Anno di inizio 2013
 Periodo (anno-mese-giorno) 2013-05-01   -   2015-10-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    Nome Ente NON disponibile

 Organization address address: COURS FAURIEL 158
city: SAINT ETIENNE CEDEX
postcode: 42023

contact info
Titolo: Mr.
Nome: Christophe
Cognome: Obidig
Email: send email
Telefono: 33442616613

FR (SAINT ETIENNE CEDEX) coordinator 269˙743.80

Mappa


 Word cloud

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

scaffolds    fibrils    diseases    structures    neurodegenerative    cell    conformational    misfolding    electric    transitions    amyloid    conformation    proteins    sensitive    beta    protein    alzheimer    proteprobe    tissue    structure   

 Obiettivo del progetto (Objective)

'ProtEprobe takes advantage of the recent cutting edge developments in protein conformation control at the Malliaras group and high sensitive protein sensing using high sensitivity factor triangular silver nanoplates by the fellow. Misfolding of a protein occurs when it becomes trapped in a local potential energy minimum where the conformation differs from the native-state structure. External electric fields have been demonstrated to distinctly alter protein secondary structures. Proteins associated with protein misfolding diseases, incuding neurodegenerative diseases such as Alzheimer's, undergo conformational changes such as the transformation of largely random coiled or α-helix structures to the highly ordered β-structures found in protein fibrils. Amyloid fibrils formed from peptide Amyloid beta (Aβ), are a major component of amyloid plaques in the brains of Alzheimer’s patients. The ProtEprobe technique will use electrical potential gradients to stimulate and control the conformation transitions of proteins including the cell adhesion protein Fibronectin and Aβ on 3D electrospun conductive polymer tissue scaffolds. The high sensitive spectral response of the nanoplate monitors will be used to analyse protein conformational transitions and observe the progression of Aβ fibril formation. Investigations will be carried out to ascertain the impact of the presence of an electric field and the capacity to tune the strength in order to enable improved understanding and selection of protein conformations on tissue scaffolds, towards enhancing cell surface interactions, healing of misfolding and facilitating the restoration of the structure and function of diseased tissues. In a paradigm step towards imparting a new dimension to tissue regeneration, ProtEprobe will develop 3D bioactive scaffolds with electrically programmable protein conformation and in situ real-time protein nanomonitors paving the way for the treatment and prevention of many neurodegenerative diseases.'

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