具有K ~+通道阻断活性的蝎毒多肽-
The electronic structure and dipole moment of charybdotoxin, a scorpion venom peptide with K+ channel blocking activity
摘要：
利用量子力学方法研究了具有钾离子通道阻断剂作用的蝎毒肽- ChTX的偶极矩矢量（145 D）可以被全长KcsA钾通道的大偶极子（403 D）搅动，从而在细胞表面上结合离子通道之前呈现适当的取向。首次揭示了ChTX前线轨道的局域化。HOMO位于Trp 14上，而三个最低能量的MO（LUMO、LUMO+1和LUMO+2）位于表征该肽的三个二硫键上。工程化ChTX的HOMO-LUMO（H-L）间隙的有效方式是用Ala 14替换其Trp 14残基，而通过插入一对L-α-氨基丁酸残基来缺失LUMO相关的二硫键不影响H-L能隙。
英文摘要：
The electronic structure of charybdotoxin (ChTX), a scorpion venom peptide that is known to act as a potassium channel blocker, is investigated with the aid of quantum mechanical calculations. The dipole moment vector (145 D) of ChTX can be stirred by the full length KcsA potassium channel's macrodipole (403 D) thereby assuming the proper orientation before binding the ion channel on the cell surface. The localization of the frontier orbitals of ChTX has been revealed for the first time. HOMO is localized on Trp14 while the three lowest-energy MOs (LUMO, LUMO+1, and LUMO+2) are localized on the three disulfide bonds that characterize this pepetide. An effective way to engineer the HOMO-LUMO (H-L) gap of ChTX is that of replacing its Trp14 residue with Ala14 whereas deletion of the LUMO-associated disulfide bond with the insertion of a pair of L-alpha-aminobutyric acid residues does not affect the H-L energy gap.
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