Baltikinin: A New Myotropic Tryptophyllin-3 Peptide Isolated from the Skin Secretion of the Purple-Sided Leaf Frog, Phyllomedusa baltea

Daning Shi,Xinping Xi,Hang Chen,Mei Zhou,Lei Wang,Yitian Gao,Tianbao Chen,Chris Shaw,Chengbang Ma

doi:10.3390/toxins8070213

Abstract

Here we report the identification of a novel tryptophyllin-3 peptide with arterial smooth muscle relaxation activity from the skin secretion of the purple-sided leaf frog, Phyllomedusa baltea. This new peptide was named baltikinin and had the following primary structure, pGluDKPFGPPPIYPV, as determined by tandem mass spectrometry (MS/MS) fragmentation sequencing and from cloned skin precursor-encoding cDNA. A synthetic replicate of baltikinin was found to have a similar potency to bradykinin in relaxing arterial smooth muscle (half maximal effective concentration (EC50) is 7.2 nM). These data illustrate how amphibian skin secretions can continue to provide novel potent peptides that act through functional targets in mammalian tissues.

Highlights

Amphibian skin secretions have provided a wide range of bioactive peptides for international biochemical and pharmacology research communities [1,2,3,4]
DiscussionMany novel peptides from amphibian skin secretions have been characterized based on chemical attributes, structure, activity in bioassays and functionality [1,2,3,4]
Pharmacological studies allow be classified from structurally and functionally offer a morehave holisticbeen approach in determining based on Manypeptides noveltopeptides amphibian skin and secretions characterized the biological role/activity of novel peptides often overlooked by previously published work

Summary

Introduction

Amphibian skin secretions have provided a wide range of bioactive peptides for international biochemical and pharmacology research communities [1,2,3,4]. Erspamer predicted that many of the peptides found in amphibian skin secretions would have endogenous regulatory counterparts in mammalian tissues—a prediction that has proven to be true [4,5,6]. Following these early studies, research has been performed on over 200 American amphibian species as well as hundreds of species from other continents. Systematic structural analysis of these skin-derived bioactive peptides has enabled researchers to assign individual peptides to previously identified families on the basis of their amino acid sequence similarities [4,8,9]

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Results

Conclusion