POLYPROT
Protein-Repellent Polymers
| Coordinatore | INSTITUT MAX VON LAUE - PAUL LANGEVIN
Organization address
address: 6 Rue Jules Horowitz contact info |
| Nazionalità Coordinatore | France [FR] |
| Totale costo | 193˙594 € |
| EC contributo | 193˙594 € |
| 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-IEF |
| Funding Scheme | MC-IEF |
| Anno di inizio | 2012 |
| Periodo (anno-mese-giorno) | 2012-04-02 - 2014-04-01 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
INSTITUT MAX VON LAUE - PAUL LANGEVIN
Organization address
address: 6 Rue Jules Horowitz contact info |
FR (GRENOBLE) | coordinator | 193˙594.80 |
Mappa
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Obiettivo del progetto (Objective)
'Protein adsorption to material surfaces causes problems in numerous technological and medical applications. A favoured approach in order to prevent protein adsoprtion is to decorate surfaces with brushes of terminally anchored, neutral water soluble polymers (NWSP). But despite the great importance of NWSP-functionalization in medicine and technology, the interaction of proteins with NWSP is not fully understood. In particular, little is known about the mechanisms responsible for regularly observed 'brush failure', where protein adsorption occurs despite NWSP functionalization. Here, we propose a systematic investigation of this phenomenon on a detailed structural level. Proteins interacting with NWSP-decorated surfaces of defined characteristics (i.e., polymer length and grafting density) will be localized using the combination of two sophisticated scattering techniques: 1) Neutron reflectometry (NR) with contrast variation. 2) Standing-wave x-ray fluorescence (SWXF). Both techniques possess un-matched spatial resolution and unique, yet complementary, chemical sensitivity. Their combination will reveal the contribution of different interaction modes of proteins with NWSP-decorated surfaces on a quantitative level. The results will provide an invaluable basis for the 'rational design' of protein-repellent surface functionalization.'
Introduzione (Teaser)
Protein adsorption to materials' surfaces creates problems in preparing or analysing solutions containing them and in in-vivo medical applications. Deeper knowledge of the interactions between proteins and repellent-treated surfaces will aid in optimising surface functionalisations.