The design of a new potent and selective ligand for the orphan bombesin receptor subtype 3 (BRS3)
Journal of Peptide Science2004Vol. 11(3), pp. 136–141
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Robert G. Boyle, John Eric Humphries, T. Andrew Mitchell, Graham A. Showell, Robert P. Apaya, Hiroaki Iijima, Hiroshi Shimada, Tomonori Arai, Hiroaki Ueno, Yoshihiro Usui, Toshiro Sakaki, Etsuko Wada, Keiji Wada
Abstract
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.
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