Structure-Activity Relationship Study of Cyclic Pentapeptide Ligands for Atypical Chemokine Receptor 3 (ACKR3)

J Med Chem. 2018 Apr 26;61(8):3745-3751. doi: 10.1021/acs.jmedchem.8b00336. Epub 2018 Apr 12.

Abstract

The atypical chemokine receptor 3 (ACKR3)/CXC chemokine receptor 7 (CXCR7) recognizes stromal cell-derived factor 1 (SDF-1)/CXCL12 and is involved in a number of physiological and pathological processes. Here, we investigated the SAR of the component amino acids in an ACKR3-selective ligand, FC313 [ cyclo(-d-Tyr-l-Arg-l-MeArg-l-Nal(2)-l-Pro-)], for the development of highly active ACKR3 ligands. Notably, modification at the l-Pro position with a bulky hydrophobic side chain led to improved bioactivity toward ACKR3.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • HEK293 Cells
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Structure
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / pharmacology*
  • Receptors, CXCR / chemistry
  • Receptors, CXCR / metabolism*
  • Structure-Activity Relationship

Substances

  • ACKR3 protein, human
  • Ligands
  • Peptides, Cyclic
  • Receptors, CXCR