colopendra subspinipes mutilans is a kind of venomous animals belonging to Chilopoda. It is widely distributed in Hubei, Jiangsu, Zhejiang and has been used as traditional medicine for thousands of years. All of them can kill insects and some small vertebrate with their venoms.In this thesis, a series of experiments were carried out to study centipede venoms. Six novel netroutoxin-like peptides were purified from Scolopendra subspinipes mutilans venoms by a two-step purification protocol including one step of gel filtra-tion and one step of RP-HPLC. Edman degradation method was used for the determination of their amino acid sequence. The determined sequence of μ-SLPTX-Ssm1a，κ-SLPTX-Ssm1a, κ-SLPTX -Ssm2a and κ-SLPTX -Ssm3a，ω-SLPTX-Ssm1a and ω-SLPTX-Ssm2a were ADNKFENSLRREIACGQCRDKVKCDPYFYHCG,TDDESSNKCAKTKRRENVCRVCGNRSGNDEYYSECCESDYRYHRCLDLLRN,AQNHYCKEHNCPPGKHCPKVPIVCVYGPCCF,EVIAIDGLEICSNDQLHVTIYSIFSPLFDKPKLNYYFNCSCPGSIYISDVYPKYFNDIAHIEYRCKLT,EECPSLSGGSSNYCSKKETFTSNGNLEQTRRYCNSVAAPSTACTDLKTGGKLCEYSCNTDGCNSVAGMEPTRAVYFIAILMLA and EESQHDTLENVEYRLSCIPKGGECERMADTCCPGLQCLGCNPFNKENLGKCKCQ respectively. We observed the effects of these neurotoxin-like peptides on the volt-age-activated tetrodotoxin-sensitive (TTX-S) sodium current and delay-rectified po-tassium current of rat DRG cells. The result showed that μ-SLPTX-Ssm1a, 3762.5Da, could inhibit TTX-S fast sodium current and has limited effects on TTX-R sodium current. The inhibitions were dose-dependent. The IC50 value of it was approximately 9 + 2 nM（n=5）. κ-SLPTX-Ssm1a, κ-SLPTX -Ssm2a and κ-SLPTX -Ssm3a are in-hibitors of KV channels，the IC50 values of κ-SLPTX-Ssm1a and κ-SLPTX -Ssm2a were 44.2 + 5.7 nM （n=5）and 570 + 126 nM （n=5） separately. ω-SLPTX-Ssm1a activates CaV channels and ω-SLPTX-Ssm2a inhibits CaV channels. ω-SLPTX-Ssm2a inhibits CaV channel currents in DRG neurons with an IC50 of about 1590 + 279nM（n=5）. In summary：Six peptide toxins from Scolopendra subspinipes mutilans have beenisolated．The structural and functional investigation proved that they are novel toxins with new amino acid sequences and specific functions targeting different ion channel. They presented the biological diversity of centipede toxins and are of significances as tools for studying neurobiology especially for investigation of ion channels．