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


  • 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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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.