2011Chinese Journal of Natural MedicinesRequires access

A Novel Bioactive Peptide with Myotropic Activity from Wasp Venoms

Yan Hong

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Abstract

AIM:To study the chemical constituents of the venom of Vespa bicolor Fabricius collected from Shanxi Province,China.METHODS:Gel chromatography and HPLC were applied to isolate a peptide from the venom.Mass spectrometry and Edman degradation were used for its structural characterization.The cDNA encoding vespin-BF precursor was cloned from the cDNA library of the venomous glands.The synthetic peptide was used for its bioassay.RESULTS:A novel bioactive peptide(vespin-BF) with unique primary structure was purified and characterized.Its amino acid sequence was determined as TYQRKMAITAGAVKHRLMSTTIIIILVRIE YLRDNMVISLESSF.Vespin-BF induced contraction of isolated ileum smooth muscle.The precursor is composed of 67 amino acid residues including the predicted signal peptide and mature vespin-BF.A di-basic enzymatic processing site(-KR-) was located between the signal and the mature peptide.BLAST search indicated that vespin-BF shows obvious similarity to vespin identified from the venoms of Vespa magnifica.CONCLUSION:A novel bioactive peptide from the wasp venoms was characterized.

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What this paper is about

AIM:To study the chemical constituents of the venom of Vespa bicolor Fabricius collected from Shanxi Province,China.METHODS:Gel chromatography and HPLC were applied to isolate a peptide from the venom.Mass spectrometry and Edman degradation were used for its structural characterization.The cDNA encoding vespin-BF precursor was cloned from the cDNA library of the venomous glands.The synthetic peptide was used for its bioassay.RESULTS:A novel bioactive peptide(vespin-BF) with unique primary structure was purified and characterized.Its amino acid sequence was determined as TYQRKMAITAGAVKHRLMSTTIIIILVRIE YLRDNMVISLESSF.Vespin-BF induced contraction of isolated ileum smooth muscle.The precursor is composed of 67 amino acid residues including the predicted signal peptide and mature vespin-BF.A di-basic enzymatic processing site(-KR-) was located between the signal and the mature peptide.BLAST search indicated that vespin-BF shows obvious similarity to vespin identified from the venoms of Vespa magnifica.CONCLUSION:A novel bioactive peptide from the wasp venoms was characterized.

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Available abstract

AIM:To study the chemical constituents of the venom of Vespa bicolor Fabricius collected from Shanxi Province,China.METHODS:Gel chromatography and HPLC were applied to isolate a peptide from the venom.Mass spectrometry and Edman degradation were used for its structural characterization.The cDNA encoding vespin-BF precursor was cloned from the cDNA library of the venomous glands.The synthetic peptide was used for its bioassay.RESULTS:A novel bioactive peptide(vespin-BF) with unique primary structure was purified and characterized.Its amino acid sequence was determined as TYQRKMAITAGAVKHRLMSTTIIIILVRIE YLRDNMVISLESSF.Vespin-BF induced contraction of isolated ileum smooth muscle.The precursor is composed of 67 amino acid residues including the predicted signal peptide and mature vespin-BF.A di-basic enzymatic processing site(-KR-) was located between the signal and the mature peptide.BLAST search indicated that vespin-BF shows obvious similarity to vespin identified from the venoms of Vespa magnifica.CONCLUSION:A novel bioactive peptide from the wasp venoms was characterized.

Key concepts: Edman degradation, Peptide, Venom, Peptide sequence, Amino acid, Signal peptide, Protein primary structure, Biology

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