Coordinatore | THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD
Organization address
address: University Offices, Wellington Square contact info |
Nazionalità Coordinatore | United Kingdom [UK] |
Totale costo | 180˙783 € |
EC contributo | 180˙783 € |
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-IEF-2008 |
Funding Scheme | MC-IEF |
Anno di inizio | 2010 |
Periodo (anno-mese-giorno) | 2010-06-01 - 2012-05-31 |
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THE CHANCELLOR, MASTERS AND SCHOLARS OF THE UNIVERSITY OF OXFORD
Organization address
address: University Offices, Wellington Square contact info |
UK (OXFORD) | coordinator | 180˙783.75 |
Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.
'Of the estimated 400 ion channels encoded in the human genome, ~70 are potassium (K) channels. Their implication in a number of human diseases, e.g., cardiac arrhythmia, cystic fibrosis, makes K channels relevant drug targets. Whereas the number of high-resolution structures of membrane proteins has consistently increased over the last few years, their functional characterization using screening approaches has not kept pace with that of water-soluble proteins. In this context, reliable and informative rapid screening assays for membrane proteins are needed. By further developing the recently reported droplet interface bilayer (DIB) system, I intend to develop a rapid automatable platform for screening wild-type channels as well as libraries of mutant ion channels using Kcv (viral), KvAP (prokaryotic) and Kv1.2 (eukaryotic) as model systems. My blueprint for such a screening device is analogous to an assembly line consisting of a network of microchannels to; (i) construct lipid monolayer-encased aqueous droplets, (ii) synthesize ion channels inside these nanobioreactors by coupled in vitro transcription-translation (IVTT), (iii) form bilayers with other droplets containing channel blockers, (iv) subsequently measure single-channel conductance to determine activity. The assay will be capable of screening one channel against hundreds of blockers or screen a library of mutants against one or a few blockers. The development of this nanoscale-streamlined process offers the possibility of producing powerful lab-on-chip instruments for membrane protein assays, which have previously proven intractable.'