PTM-FLEX

Synthetic biology approach for the design of new-to-nature peptide-based antibiotic molecules

Coordinatore	EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZURICH    more  Organization address address: Raemistrasse 101 city: ZUERICH postcode: 8092 contact info Titolo: Prof. Nome: Sven Cognome: Panke Email: send email Telefono: +41 61 3873121
Nazionalità Coordinatore	Switzerland [CH]
Totale costo	199˙317 €
EC contributo	199˙317 €
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-2013-IEF
Funding Scheme	MC-IEF
Anno di inizio	2014
Periodo (anno-mese-giorno)	2014-04-15   -   2016-04-14

 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: Sven Cognome: Panke Email: send email Telefono: +41 61 3873121	CH (ZUERICH)	coordinator	199˙317.60

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 Obiettivo del progetto (Objective)

'The rise of pathogenic bacteria that are resistant against a variety of antibiotic treatment emphasizes the need for novel active molecules. One promising novel class of active molecules is genetically encoded and ribosomally synthesized peptides, as they offer the potential to employ directed evolution approaches across a huge sequence space directly on an active substance in order to engineer novel activities and thus introduce a novel engineering principle into antibiotic development. However, in many cases the activity of the peptide molecule depends on substantial posttranslational modifications (PTMs) which give the peptides conformational stability and protect against proteolytic degradation. Consequently, the degrees of freedom in the engineering of such peptides on sequence level are highly dependent on the flexibility of the PTM-machinery to accept such changes. Here, we propose a synthetic biology approach to study systematically the flexibility of PTM-machineries for the class of lanthipepetides in order to assemble a highly flexible machinery that will support a broad range of engineering measures and thus optimize the chances to discover molecules with modified or completely novel activities. We also propose to implement a high-throughput screen for the bioactivity of these molecules in order to be able to engineer specific enzymes of the PTM-machinery for increased flexibility and to finally implement large scale directed evolution screens for novel antibiotic activities.'