A Conformationally Frozen Peptoid Boosts CXCR4 Affinity and Anti-HIV Activity

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 highe...

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Bibliographic Details
Published inAngewandte Chemie International Edition Vol. 51; no. 32; pp. 8110 - 8113
Main Authors Demmer, Oliver, Frank, Andreas O., Hagn, Franz, Schottelius, Margret, Marinelli, Luciana, Cosconati, Sandro, Brack-Werner, Ruth, Kremb, Stephan, Wester, Hans-Jürgen, Kessler, Horst
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 06.08.2012
WILEY‐VCH Verlag
Wiley
Wiley Subscription Services, Inc
EditionInternational ed. in English
Subjects
Affinity
Anti-HIV Agents - pharmacology
Binding
biological activity
Chains
Chemistry
Chemistry, Multidisciplinary
Chemokine receptors
drug design
Freezing
Frozen
HIV-1 - drug effects
Human immunodeficiency virus
Human immunodeficiency virus 1
Humans
Ligands
medicinal chemistry
Models, Molecular
Molecular Conformation
Nitrogen atoms
peptides
peptidomimetics
Peptoids - chemistry
Peptoids - pharmacology
Physical Sciences
Pictures
Receptors, CXCR4 - agonists
Receptors, CXCR4 - metabolism
Science & Technology
Structure-Activity Relationship
CELLS
biological activity
drug design
CHEMOKINE RECEPTOR CXCR4
AMD3100
peptides
LESTR/FUSIN
DISCOVERY
peptidomimetics
INFECTION
LIGAND
INHIBITORS
ANTAGONISTS
medicinal chemistry
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Summary: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.
Bibliography:ArticleID:ANIE201202090
We thank M. Wolff and B. Cordes for technical assistance and E. Gourni for the help in the cell binding assay. This work was supported by the Center of Integrated Protein Science Munich (CIPS). Financial support by the DFG (SFB824, Subproject B5) is acknowledged. The representation of the HI virus in the Table of Contents graphic was originally created by the US National Institute of Health (Permission: PD-USGov-HHS-NIH)
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DFG
ark:/67375/WNG-M8R46FS1-4
We thank M. Wolff and B. Cordes for technical assistance and E. Gourni for the help in the cell binding assay. This work was supported by the Center of Integrated Protein Science Munich (CIPS). Financial support by the DFG (SFB824, Subproject B5) is acknowledged. The representation of the HI virus in the Table of Contents graphic was originally created by the US National Institute of Health (Permission: PD‐USGov‐HHS‐NIH)
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SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201202090