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Demmer, O.* ; Frank, A.O.* ; Hagn, F.* ; Schottelius, M.* ; Marinelli, L.* ; Cosconati, S.* ; Brack-Werner, R. ; Kremb, S. ; Wester, H.J.* ; Kessler, H.*

A conformationally frozen peptoid boosts CXCR4 affinity and anti-HIV activity.

Angew. Chem.-Int. Edit. 51, 8110-8113 (2012)
Verlagsversion Volltext DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
There can be only one: Using a peptoid motif obtained by shifting the arginine side chain of a pentapeptide previously developed by Fujii et al. to the neighboring nitrogen atom restricts the conformational freedom and yields a conformationally homogeneous peptide (see picture) with a 100-fold higher binding affinity to the chemokine receptor CXCR4 in the picomolar range. Its efficiency to inhibit HIV-1 infections is also demonstrated. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Biological Activity ; Drug Design ; Medicinal Chemistry ; Peptides ; Peptidomimetics; Chemokine Receptor CXCR4; Peptides; AMD3100; Antagonists; Discovery; Infection; Ligand; Cells; Lestr/Fusin; Inhibitors
ISSN (print) / ISBN 1433-7851
e-ISSN 1521-3773
Quellenangaben Band: 51, Heft: 32, Seiten: 8110-8113 Artikelnummer: , Supplement: ,
Verlag Wiley
Verlagsort Weinheim
Begutachtungsstatus Peer reviewed