| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2526627 | Chinese Journal of Natural Medicines | 2011 | 4 Pages |
AimTo study the chemical constituents of the venom of Vespa bicolor Fabricius collected from Shanxi Province, China.MethodsGel 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.ResultsA 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.ConclusionA novel bioactive peptide from the wasp venoms was characterized.
