PROTENGENCTRANS

Protein engineering for encapsulation and intracellular transport

Coordinatore	EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZURICH    more  Organization address address: Raemistrasse 101 city: ZUERICH postcode: 8092 contact info Titolo: Prof. Nome: Donald Cognome: Hilvert Email: send email Telefono: +41 44 632 3176 Fax: +41 44 632 1486
Nazionalità Coordinatore	Switzerland [CH]
Totale costo	0 €
EC contributo	181˙368 €
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	2009
Periodo (anno-mese-giorno)	2009-04-01   -   2011-03-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZURICH  Organization address address: Raemistrasse 101 city: ZUERICH postcode: 8092 contact info Titolo: Prof. Nome: Donald Cognome: Hilvert Email: send email Telefono: +41 44 632 3176 Fax: +41 44 632 1486	CH (ZUERICH)	coordinator	181˙368.45

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 Obiettivo del progetto (Objective)

'The main goal of this project is to develop a system for effective encapsulation and transport of negatively charged guests into living cells using an enginnered protein capsid. The research in prof. Hilvert's group demonstrated that it is possible to engineer the inner surface of a capsid formed by lumazine synthase from Aquifex aeolicus (AaLS) to accept positively charged guests while retaining the icosahedral structure. In my project I will be addressing the following issues: - Engineering the inner surface of the AaLS to express positively charged aminoacid residues maintaining the ability of the mutant to form an icosahedral capsid - Investigating stability and potential selectivity of guest encapsulation by the modified capsid - Attaching a delivery tag to the outer surface of the capsid in order to make it cell-permeable - Enabling efficient release of the cargo after cellular uptake, by attaching a degradation tag. The proposed project will provide us with a complete system for coating, intracellular transport and release of negatively charged biomolecules. It will be used to internalize membrane-impermeable molecules like siRNA, negatively charged GFP, and in perspective other proteins or oligonucleotide-based molecules. Based on our results, novel systems for regulating gene expression and investigating mechanisms of RNA interference may be developed. The use of a protein as the encapsulating agent will help to overcome shortages of existing systems for gene therapy using viral vectors, like mutagenesis or immune response. It raises hope for future medical applications of our results.'