Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima

Tianbao Chen; M. O’Rourke; D.F. Orr; D.J.M. Coulter; David Hirst; P.F. Rao; Christopher Shaw

doi:10.1016/j.regpep.2003.08.003

Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima

Tianbao Chen
, M. O’Rourke
, D.F. Orr
, D.J.M. Coulter
, David Hirst
, P.F. Rao
, Christopher Shaw

School of Pharmacy

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

We have isolated a novel bradykinin B2-receptor antagonist peptide, kinestatin, from toad (Bombina maxima) defensive skin secretion. Mass spectroscopy established a molecular mass of 931.56 Da and a provisional structure: pGlu-Leu/Ile-Pro-Gly-Leu/Ile-Gly-Pro-Leu/Ile-Arg.amide. The unmodified sequence, -QIPGLGPLRG-, was located at the C-terminus of a 116-amino-acid residue open-reading frame following interrogation of a sequenced B. maxima skin cDNA library database. This confirmed the presence of appropriate primary structural attributes for the observed post-translational modifications present on the mature peptide and established residue 2 as Ile and residues 5/8 as Leu. Kinestatin represents a prototype novel peptide from amphibian skin.

Original language	English
Pages (from-to)	147-154
Number of pages	8
Journal	Regulatory Peptides
Volume	116
Issue number	1-3
DOIs	https://doi.org/10.1016/j.regpep.2003.08.003
Publication status	Published - 15 Nov 2003

ASJC Scopus subject areas

Biochemistry
Endocrinology
Physiology
General Neuroscience

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title = "Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima",

abstract = "We have isolated a novel bradykinin B2-receptor antagonist peptide, kinestatin, from toad (Bombina maxima) defensive skin secretion. Mass spectroscopy established a molecular mass of 931.56 Da and a provisional structure: pGlu-Leu/Ile-Pro-Gly-Leu/Ile-Gly-Pro-Leu/Ile-Arg.amide. The unmodified sequence, -QIPGLGPLRG-, was located at the C-terminus of a 116-amino-acid residue open-reading frame following interrogation of a sequenced B. maxima skin cDNA library database. This confirmed the presence of appropriate primary structural attributes for the observed post-translational modifications present on the mature peptide and established residue 2 as Ile and residues 5/8 as Leu. Kinestatin represents a prototype novel peptide from amphibian skin.",

author = "Tianbao Chen and M. O{\textquoteright}Rourke and D.F. Orr and D.J.M. Coulter and David Hirst and P.F. Rao and Christopher Shaw",

year = "2003",

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doi = "10.1016/j.regpep.2003.08.003",

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T1 - Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima

AU - Chen, Tianbao

AU - O’Rourke, M.

AU - Orr, D.F.

AU - Coulter, D.J.M.

AU - Hirst, David

AU - Rao, P.F.

AU - Shaw, Christopher

PY - 2003/11/15

Y1 - 2003/11/15

N2 - We have isolated a novel bradykinin B2-receptor antagonist peptide, kinestatin, from toad (Bombina maxima) defensive skin secretion. Mass spectroscopy established a molecular mass of 931.56 Da and a provisional structure: pGlu-Leu/Ile-Pro-Gly-Leu/Ile-Gly-Pro-Leu/Ile-Arg.amide. The unmodified sequence, -QIPGLGPLRG-, was located at the C-terminus of a 116-amino-acid residue open-reading frame following interrogation of a sequenced B. maxima skin cDNA library database. This confirmed the presence of appropriate primary structural attributes for the observed post-translational modifications present on the mature peptide and established residue 2 as Ile and residues 5/8 as Leu. Kinestatin represents a prototype novel peptide from amphibian skin.

AB - We have isolated a novel bradykinin B2-receptor antagonist peptide, kinestatin, from toad (Bombina maxima) defensive skin secretion. Mass spectroscopy established a molecular mass of 931.56 Da and a provisional structure: pGlu-Leu/Ile-Pro-Gly-Leu/Ile-Gly-Pro-Leu/Ile-Arg.amide. The unmodified sequence, -QIPGLGPLRG-, was located at the C-terminus of a 116-amino-acid residue open-reading frame following interrogation of a sequenced B. maxima skin cDNA library database. This confirmed the presence of appropriate primary structural attributes for the observed post-translational modifications present on the mature peptide and established residue 2 as Ile and residues 5/8 as Leu. Kinestatin represents a prototype novel peptide from amphibian skin.

UR - https://www.scopus.com/pages/publications/0242361253

U2 - 10.1016/j.regpep.2003.08.003

DO - 10.1016/j.regpep.2003.08.003

M3 - Article

SN - 0167-0115

VL - 116

SP - 147

EP - 154

JO - Regulatory Peptides

JF - Regulatory Peptides

IS - 1-3

ER -

Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima

Abstract

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