FMP Publications

Our publications are recorded in a searchable database since 2010, updates will be added regularly.

Year:  
All :: 2015
Author:  
All :: (, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z 
All :: Haag(*), ... , Hennig(*), Henning(*), Hennings(*), ... , Hyvl(*) 
Preferences: 
References per page: Show keywords Show abstracts
References
Exploring monovalent and multivalent peptides for the inhibition of FBP21-tWW
Henning(*), L. M., Bhatia(*), S., Bertazzon(*), M., Marczynke(*), M., Seitz(*), O., Volkmer, R., Haag(*), R.; Freund(*), C.
Beilstein J Org Chem, 11:701-706
(2015)

Tags: Peptide Synthesis (Hackenberger/Volkmer)

Abstract: The coupling of peptides to polyglycerol carriers represents an important route towards the multivalent display of protein ligands. In particular, the inhibition of low affinity intracellular protein-protein interactions can be addressed by this design. We have applied this strategy to develop binding partners for FBP21, a protein which is important for the splicing of pre-mRNA in the nucleus of eukaryotic cells. Firstly, by using phage display the optimized sequence WPPPPRVPR was derived which binds with K Ds of 80 muM and 150 microM to the individual WW domains and with a K D of 150 muM to the tandem-WW1-WW2 construct. Secondly, this sequence was coupled to a hyperbranched polyglycerol (hPG) that allowed for the multivalent display on the surface of the dendritic polymer. This novel multifunctional hPG-peptide conjugate displayed a K D of 17.6 microM which demonstrates that the new carrier provides a venue for the future inhibition of proline-rich sequence recognition by FBP21 during assembly of the spliceosome.

Export as:
BibTeX, XML

Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Germany
+4930 94793 - 100 
+4930 94793 - 109 (Fax)
info(at)fmp-berlin.de

Like many sites, we use cookies to optimize the user's browsing experience. Data Protection OK