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Open Access Green as soon as Postprint is submitted to ZB.
A conformationally frozen peptoid boosts CXCR4 affinity and anti-HIV activity.
Angew. Chem.-Int. Edit. 51, 8110-8113 (2012)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
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
Volume: 51,
Issue: 32,
Pages: 8110-8113
Publisher
Wiley
Publishing Place
Weinheim
Reviewing status
Peer reviewed
Institute(s)
Institute of Virology (VIRO)