Abdel-Mottaleb Yousra, Vandendriessche Thomas, Clynen Elke, Landuyt Bart, Jalali Amir, Vatanpour Hossein, Schoofs Liliane, Tytgat Jan
Laboratory of Toxicology, University of Leuven, Onderwijs and Navorsing II, Herestraat 49, Leuven, Belgium.
Toxicon. 2008 Jun 15;51(8):1424-30. doi: 10.1016/j.toxicon.2008.03.027. Epub 2008 Mar 29.
The first Kv1.3 channel-selective toxin from the venom of the Iranian scorpion Odonthobuthus doriae (OdK2) was purified, sequenced and characterized physiologically. OdK2 consists of 38 amino acids, including six conserved cysteine and a C-terminal lysine residue, as revealed by the unique use of a quadrupole ion cyclotron resonance Fourier-transform mass spectrometer. Based on multiple sequence alignments, OdK2 was classified as alpha-KTX3.11. The pharmacological effects of OdK2 were studied on a panel of eight different cloned K(+) channels (vertebrate Kv1.1-Kv1.6, Shaker IR and hERG) expressed in Xenopus laevis oocytes. Interestingly, OdK2 selectively inhibits the currents through Kv1.3 channels with an IC50 value of 7.2+/-2.7nM.
从伊朗蝎子奥氏钝绥螨(OdK2)毒液中分离出首个Kv1.3通道选择性毒素,并对其进行了纯化、测序及生理特性鉴定。四极杆离子回旋共振傅里叶变换质谱仪的独特应用显示,OdK2由38个氨基酸组成,包括6个保守的半胱氨酸和1个C端赖氨酸残基。基于多序列比对,OdK2被归类为α-KTX3.11。研究了OdK2对非洲爪蟾卵母细胞中表达的8种不同克隆K(+)通道(脊椎动物Kv1.1-Kv1.6、Shaker IR和hERG)的药理作用。有趣的是,OdK2以7.2±2.7nM的IC50值选择性抑制通过Kv1.3通道的电流。