The design of a new potent and selective ligand for the orphan bombesin receptor subtype 3 (BRS3)

J Pept Sci. 2005 Mar;11(3):136-41. doi: 10.1002/psc.599.


Extensive SAR studies on the unselective BRS3 agonist, [H-D-Phe6,beta-Ala11,Phe13,Nle14]-bombesin-(6-14)-nonapeptide amide, have highlighted structural features important for BRS3 activity and have provided guidance as to the design of selective agonists. A radically modified heptapeptide agonist, maintaining only the Trp-Ala moiety of the parent [H-D-Phe6,betaAla11,Phe13,Nle14]-peptide amide, and with a very different carboxyl terminal region, has been produced which was potent at BRS3 and essentially had no NMB or GRP receptor activity. Its structure is Ac-Phe-Trp-Ala-His(tauBzl)-Nip-Gly-Arg-NH2.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bombesin / analogs & derivatives*
  • Bombesin / chemical synthesis
  • Bombesin / chemistry
  • Cell Line
  • Drug Design*
  • Humans
  • Ligands
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, Bombesin / agonists*
  • Receptors, Bombesin / metabolism*
  • Substrate Specificity


  • Ligands
  • Receptors, Bombesin
  • bombesin receptor subtype 3
  • Bombesin