NATURAL PRODUCT RESEARCH AND DEVELOPMENT ›› 2019, Vol. 31 ›› Issue (9): 1596-1601.doi: 10.16333/j.1001-6880.2019.9.017

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Determination of peptide and protein diversity in venom of Vespa magnifica（Smith）on structure and function

ZHOU Si-tong1,2,CHE Yi-hao1,2,NI Lian-li1,2,LI Long-xing3,4,YUAN Shi-meng1,2,YANG Zi-zhong1,2,3,YANG Zhi-bin1,2,3*,ZHANG Cheng-gui1,2,3*   

  1. 1Yunnan Provincial Key Laboratory of Entomological Biopharmaceutical R&D,Dali University; 2National-local Joint Engineering Research center of Entomoceutics,Dali University; 3Yunnan Provincial Collaborative Innovation Center for Entomoceutics,Dali University; 4Analyzing and Testing Center,Dali University,Dali 671000,China
  • Online:2019-10-09 Published:2019-10-23
  • Supported by:

    国家自然科学基金（81360679）；云南省应用基础研究青年项目(2016FD074)；云南省科技创新平台建设项目(2015DG030)

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Abstract: In order to prove that Vespa magnifica (Smith) venom has great medicinal purposes development value.In this study,the distribution of molecular mass of peptides and proteins was analyzed by Ultra Performance Liquid Chromatography-Electrospray-Quadrupole-Time of Flight Mass Spectrometry (UPLC-ESI-Q-TOF-MS) and Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).The relative molecular mass of the proteins is mainly distributed in the range of 17 to 45 kDa.The peptides present a unimodal distribution and 61% of them are in the range of 500-3 000 Da,which is the most abundant part of the crude venom of V. magnifica.The antibacterial activity of the venom was studied by Oxford Cup method.HepG2 human hepatoma cells and B16 melanoma cells were used as the research object to evaluate the cytotoxic activity of the venom by MTT assay,which proved the potential antibacterial activity and cytotoxic activity.The results have similarities and specific differences with other reported bees and wasp,showing the molecular diversity of the venom and providing reference for the subsequent material research and medicinal value development of the venom.

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