A refined agonist pharmacophore for protease activated receptor 2

Grant D. Barry, Jacky Y. Suen, Heng Boon Low, Bernhard Pfeiffer, Bernadine Flanagan, Maria Halili, Giang T. Le, David P. Fairlie

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17 Citations (Scopus)

Abstract

Protease activated receptor 2 (PAR2) is a G protein-coupled receptor implicated in inflammation and cancer. Only a few peptide agonists are known with greater potency than the native agonist SLIGRL-NH2. Here we report 52 peptide agonists of PAR2, 26 with activity at sub-micromolar concentrations, and one being iodinated for radioligand experiments. Potency was highest when the N- or C-termini of SLIGRL-NH2 were modified, pointing to a new ligand pharmacophore model that may aid development of drug-like PAR2 modulators.

Original languageEnglish
Pages (from-to)5552-5557
Number of pages6
JournalBioorganic and Medicinal Chemistry Letters
Volume17
Issue number20
DOIs
Publication statusPublished - 15 Oct 2007
Externally publishedYes

Keywords

  • Agonist
  • Fluorescence
  • Inflammation
  • PAR

Cite this

Barry, G. D., Suen, J. Y., Low, H. B., Pfeiffer, B., Flanagan, B., Halili, M., Le, G. T., & Fairlie, D. P. (2007). A refined agonist pharmacophore for protease activated receptor 2. Bioorganic and Medicinal Chemistry Letters, 17(20), 5552-5557. https://doi.org/10.1016/j.bmcl.2007.08.026