Bufokinin: a substance P-related peptide from the gut of the toad,Bufo marinus with high binding affinity but low selectivity for mammalian tachykinin receptors

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Abstract

A tachykinin peptide, termed bufokinin, was isolated in pure form from an extract of the intestine of the toad, Bufo marinus, and its primary structure was established as: Lys-Pro-Arg-Pro-Asp-Gln-Phe-Tyr-Gly-Leu-Met.NH2. This sequence was confirmed by chemical synthesis and shows four amino acid substitutions(Arg1 → Lys,Lys3 → Arg,Gln5 → Asp and Phe8 → Tyr) compared with substance P. Binding parameters for synthetic bufokinin and mammalian tachykinins were compared using receptor-selective radioligands and crude membranes from rat tissues enriched in the NK-1 (submandibular gland) , NK-2 (stomach fundus) and NK-3 (brain) receptors. In terms of inhibiting the binding of the selective radioligands, bufokinin (Kd = 0.3 nM) was 1.8-fold more potent than substance P at the rat NK-1 site, but it was only 2-fold less potent(Kd = 2.8 nM) than neurokinin A at the NK-2 site and only 2-fold less potent (Kd = 48 nM) than neurokinin B at the NK-3 site. Thus, bufokinin shows relatively high affinity but lack of selectivity for all three tachykinin binding sites in rat tissues.

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