LXWAP

Re-designing zinc finger proteins by swapping alpha-helical domains with foldamer helices

Coordinatore	UNIVERSITE DE BORDEAUX    more  Organization address address: PLACE PEY BERLAND 35 city: BORDEAUX postcode: 33000 contact info Titolo: Mrs. Nome: Patricia Cognome: Dulor Email: send email Telefono: 33540006802 Fax: 33540002200
Nazionalità Coordinatore	France [FR]
Totale costo	194˙046 €
EC contributo	194˙046 €
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-2012-IEF
Funding Scheme	MC-IEF
Anno di inizio	2013
Periodo (anno-mese-giorno)	2013-03-11   -   2015-03-10

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	UNIVERSITE DE BORDEAUX  Organization address address: PLACE PEY BERLAND 35 city: BORDEAUX postcode: 33000 contact info Titolo: Mrs. Nome: Patricia Cognome: Dulor Email: send email Telefono: 33540006802 Fax: 33540002200	FR (BORDEAUX)	coordinator	194˙046.60
2	UNIVERSITE BORDEAUX I  Organization address address: 351 Cours de la Liberation city: TALENCE postcode: 33405 contact info Titolo: Mrs. Nome: Patricia Cognome: Dulor Email: send email Telefono: 33540006802 Fax: 33540002200	FR (TALENCE)	participant	0.00

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 Obiettivo del progetto (Objective)

'Alpha-helices (aHs) are recurrent structures in proteins, whose folding properties, stability and function have been widely investigated. They often play the key role of recognition elements between proteins, or proteins and nucleic acids. These interactions are generally regulated by the strategic presentation of a few key residues on their surface. The efforts of many groups have been devoted to the synthesis of artificial molecules (foldamers), to mimic the structural complexity of natural helices, with the aim to reproduce their functions. A number of foldamer backbones has been synthesized to date, and their predictability and tunability constitute a great potential for their future applications. However, attaining more complex tertiary/quaternary structures through foldamers is still partially unaccomplished, and constitutes one of the ultimate goals in the field. This project will move a step forward towards the realization of this mission, by creating new composite proteins, swapping aHs with oligourea helices. The first target will be zinc fingers, a well described class of metalloproteins specialized in nucleic acid binding. Their peculiar folding, extensive structural characterization and biological relevance will be an ideal starting point to study the influence of the replacement of aHs with foldamers in this complex machinery. The new composite proteins will be tested to obtain insights into folding, metal complexation, DNA binding ability and cellular behavior of these new entities. This project will form a bridge between the expertise of the applicant in the chemistry of DNA targeting, and the host in oligourea foldamers. A further collaboration with a specialist in metallopeptides will provide the appropriate combination of knowledge required for this multidisciplinary study. This technology will be a milestone in the design of composite proteins and their use in the modulation of protein characteristics, with possible biomedical applications.'