Abstract：Abstract: Voltage-gated sodium channel Nav1.7 is preferentially expressed in peripheral nociceptors. Clinical genetics，animal models and pharmacological studies indicate that Nav1.7 is an important target for analgesic drug development. In this paper，we report the isolation and characterization of APTX-1，a novel peptide toxin from the venom of spider Calommata signata Karsch. Patch-clamp analysis confirmed that APTX-1 potently inhibits the currents of Nav1.7. Mass spectrum results showed that the molecular weight of APTX-1 was 7 815.2 Da. The first 10 amino acid positions at the N terminal were ASCKQVGEEC. APTX-1 inhibited Nav1.7 currents in a concentration-dependent manner，with a half-inhibitory concentration of (0.46±0.08) μmol/L. Channel dynamics analysis showed that APTX-1 did not affect the reversal potential，voltage-dependent steady-state activation curve，and inactivation curve of Nav1.7，indicating that the peptide toxin did not affect the ion selectivity and voltage dependence of Nav1.7. In conclusion，we found a novel Nav1.7 peptide inhibitor，and the characteristics of its action on Nav1.7 were studied to provide lead molecules for the development of analgesic drugs targeting the Nav1.7.
Key words: Calommata signata Karsch; peptide toxin; Nav1.7; APTX-1; pain
（Acta Laser Biology Sinica, 2023, 32(2): 139-145）
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引用本文:
罗 森，杨 坤，李 闽，肖文萱，雷 伟，张紫萱，陈敏芝. 一种来源于蜘蛛毒液的新型Nav1.7多肽抑制剂的发现与鉴定[J]. 激光生物学报, 2023, 32(2): 139-145.
LUO Sen, YANG Kun, LI Min, XIAO Wenxuan, LEI Wei, ZHANG Zixuan, CHEN Minzhi. Discovery and Identification of a Novel Nav1.7 Peptide Inhibitor from Spider Venom. journal1, 2023, 32(2): 139-145.
