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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Communication
A Conformationally Frozen Peptoid Boosts CXCR4 Affinity and Anti-HIV Activity†
Article first published online: 3 JUL 2012
DOI: 10.1002/anie.201202090
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Demmer, O., Frank, A. O., Hagn, F., Schottelius, M., Marinelli, L., Cosconati, S., Brack-Werner, R., Kremb, S., Wester, H.-J. and Kessler, H. (2012), A Conformationally Frozen Peptoid Boosts CXCR4 Affinity and Anti-HIV Activity. Angew. Chem. Int. Ed., 51: 8110–8113. doi: 10.1002/anie.201202090
- †
Publication History
- Issue published online: 1 AUG 2012
- Article first published online: 3 JUL 2012
- Manuscript Revised: 2 MAY 2012
- Manuscript Received: 16 MAR 2012
Funded by
- DFG
Keywords:
- biological activity;
- drug design;
- medicinal chemistry;
- peptides;
- peptidomimetics
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.