A mount of natural medicines exert their activities depending on not only small molecular compounds but also proteins and/or peptides. Recently, the group supervised by prof. Ren Lai, from Kunming Institute of Zoology, Chinese Academy of Sciences has achieved a great contribution to investigate functional proteins and peptides from medicinal insects and amphibians by proteomics and/or peptidomics combined with pharmacological test (Mol Cell Proteomics 2007, 6:882-894; 2008, 7:582-590; 2009, 8:2071-2079; 2009, 8:571-583).

Recently, they cooperated with Prof. Songping Liang from Hunan Normal University, China and Prof. King. F. Glenn from The University of Qeensland, Austraila, to study the diversity of centipede neurotoxins acting on ion channels. Twenty-six neurotoxin-like peptides belonging to ten groups were identified from the centipede venoms, Scolopendra subspinipes mutilans L. Koch. Several neurotoxins contain potential insecticidal abilities and they are found to act on voltage-gated sodium, potassium, and calcium channels, respectively. In almost all cases the primary structures of the centipede-venom peptides are unique. This represents an interesting case of convergent evolution in which different venomous animals have evolved different molecular strategies for targeting the same ion channels in prey and predators. Moreover, the high level of biochemical diversity revealed in this study suggests that centipede venoms might be attractive subjects for prospecting and screening for peptide candidates with potential pharmaceutical or agrochemical applications. The results were published in the journal of Molecular & Cellular Proteomics as a article authored by Shilong Yang, et al (Chemical punch packed in venoms makes centipedes excellent predators, http://www.mcponline.org/content/early/2012/05/17/mcp.M112.018853) .

This work was supported by the Ministry of Science and Technology (2010CB529800), Chinese National Natural Science Foundation (31070701, 31000962, 31025025)..