D/L-PEPTIDE LIBRARY

Antibacterial lead discovery with D/L-peptide libraries

 Coordinatore MAX PLANCK GESELLSCHAFT ZUR FOERDERUNG DER WISSENSCHAFTEN E.V. 

 Organization address address: Hofgartenstrasse 8
city: MUENCHEN
postcode: 80539

contact info
Titolo: Ms.
Nome: Barbara
Cognome: Dobruchowski
Email: send email
Telefono: -2822
Fax: -2914

 Nazionalità Coordinatore Germany [DE]
 Totale costo 127˙813 €
 EC contributo 127˙813 €
 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) 2009-09-01   -   2010-06-30

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    MAX PLANCK GESELLSCHAFT ZUR FOERDERUNG DER WISSENSCHAFTEN E.V.

 Organization address address: Hofgartenstrasse 8
city: MUENCHEN
postcode: 80539

contact info
Titolo: Ms.
Nome: Barbara
Cognome: Dobruchowski
Email: send email
Telefono: -2822
Fax: -2914

DE (MUENCHEN) coordinator 127˙813.76

Mappa


 Word cloud

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ligands    protein    pairing    interaction    macromolecular   

 Obiettivo del progetto (Objective)

'Nowadays, a multitude of examples for targeting enzymes with small molecules is known, whereas the direkt access to macromolecular interaction, such as DNA/protein, RNA/protein and protein/protein within the cell still waits to be solved by generic methods. We intend to create a toolbox for targeting these interactions with D-/L-peptides, a new class of biostable oligomer ligands. Initially we will establish split-and-pool libraries using postsynthetic dimerization of two orthogonal pairing partners which can be expected to form stable folds of the size of interactive protein subdomains. In a second approach, specific target functions and interaction domains will be used to generate new ligands by design and structural analogy. Folding and secondary structure preference of the most potent constructs will be elucidated (CD, NMR, FRET) to deduce preferences for pairing, minimal sequence length, and composition. Macromolecular targets and activity will be further studied using fluorescence microscopy and protein binding assays.'

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