• Port-a-Patch

    世界最小パッチクランプセットアップ
  • Port-a-Patch

    誰でもデータ取得 - 教育ツールとして最適
  • Port-a-Patch

    細胞, オルガネラ, 脂質二分子膜
  • Port-a-Patch

    世界で最も歴史あるプレーナー式パッチクランプ装置
  • Port-a-Patch

    細胞内灌流実験に最適

2020 - Trp, a conserved aromatic residue crucial to the interaction of a scorpion peptide with sodium channels

icon pap   Port-a-Patch Publication found in The Journal of Biochemistry (2020)

Authors:
Xu Y., Sun J., Yu Y., Kong X., Meng X., Liu Y., Cui Y., Su Y., Zhao M., Zhang J. 

Journal:
The Journal of Biochemistry (2020) doi: 10.1093/jb/mvaa088


Abstract:

Antitumor-analgesic peptide (AGAP), one scorpion toxin purified from Buthus martensii Karsch, was known as its analgesic and antitumor activities. Trp38, a conserved aromatic residue of AGAP, might play important roles in its interaction with sodium channels. In this study, a mutant W38F was generated and effects of W38F were examined on hNav1.4, hNav1.5, and hNav1.7 by using whole cell patch clamp, which were closely associated to the biotoxicity of skeletal and cardiac muscles, and pain signaling. The data showed that W38F decreased the inhibition effects of peak currents of hNav1.7, hNav1.4, and hNav1.5 compared with AGAP, notably, W38F reduced the analgesic activity compared with AGAP. The results suggested that Trp38 be a crucial amino acid involved in the interaction with these three sodium channels. The decreased analgesic activity of W38F might result from its much less inhibition of hNav1.7. These findings provided more information about the relationship between structure and function of AGAP and may facilitate the modification of other scorpion toxins with pharmacological effects.


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