AEOM

Constructing an Artificial Enzyme for Olefin Metathesis

Coordinatore	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 31 76 Fax: +41 44 632 14 86
Nazionalità Coordinatore	Non specificata
Totale costo	179˙297 €
EC contributo	179˙297 €
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-PEOP
Anno di inizio	2008
Periodo (anno-mese-giorno)	2008-03-01   -   2010-02-28

 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 31 76 Fax: +41 44 632 14 86	CH (ZUERICH)	coordinator	0.00

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 Obiettivo del progetto (Objective)

'The introduction of stable and selective catalysts for olefin metathesis (OM) has considerably simplified the construction of double bonds. Herein we propose to tackle two areas of the OM reaction that have received little attention. First, we will address selectivity problems in an important type of OM reaction: metathesis cross-coupling or simply cross metathesis (CM). Second, we will examine the potential applications of OM in chemical biology. OM has no biological counterpart and therefore it may be possible to do metathesis chemistry in the biological milieu without affecting endogenous cellular processes. Although seemingly incongruent goals, both are attainable within the framework of this proposal because of the special nature of the metathesis catalysts we propose to develop: artificial metathesis enzymes. We propose to endow a protein with an OM active-site. A highly modular proteinaceous secondary ligand sphere will allow the use of recombinant molecular biology techniques to generate new ligands for the metathesis catalyst; in this way a large number of catalyst structures can be generated in a short time. The family of catalysts can then be tested in metathesis reactions that are difficult to perform selectively, such as cross metathesis. A hallmark of enzymes is the exquisite selectivity they often display for their substrate, and we believe this can be harnessed in the context of OM to solve many of the current selectivity problems. A second focus of the research will be the application of the metathesis enzyme as a tool for chemical biology. Since there is no biological analogue of OM, it may be possible to use metathesis to tag biomolecules in vivo. Moreover, a protein derived ligand would allow for selective localization in vivo through the selection of an appropriate protein tag.'