Batenburg A M, Bougis P E, Rochat H, Verkleij A J, de Kruijff B
Biochemistry. 1985 Dec 3;24(25):7101-10. doi: 10.1021/bi00346a013.
The interaction of cardiotoxin II of Naja mossambica mossambica with cardiolipin model membranes was investigated by binding, fluorescence, resonance energy transfer, fluorescence quenching, 31P NMR, freeze-fracture, and small-angle X-ray experiments. An initially electrostatic binding appeared to be accompanied by a deep penetration, most likely into the acyl chain region of the phospholipids, indicating a hydrophobic contribution to the strong interaction (KD congruent to 5 X 10(-8) M). This binding results in a fusion of unilamellar vesicles as indicated by a fluorescence-based fusion assay, freeze-fracture, and X-ray diffraction. In these fused structures freeze-fracture electron microscopy reveals the appearance of particles, which is accompanied by the induction of an isotropic component in 31P NMR. The well-defined particles are interpreted as inverted micelles, and the localization of the cardiotoxin molecule in these structures is discussed.
通过结合、荧光、共振能量转移、荧光猝灭、³¹P NMR、冷冻蚀刻和小角X射线实验，研究了莫桑比克射毒眼镜蛇心脏毒素II与心磷脂模型膜的相互作用。最初的静电结合似乎伴随着深入渗透，很可能进入磷脂的酰基链区域，这表明疏水作用对强相互作用有贡献（KD约为5×10⁻⁸ M）。如基于荧光的融合测定、冷冻蚀刻和X射线衍射所示，这种结合导致单层囊泡融合。在这些融合结构中，冷冻蚀刻电子显微镜揭示了颗粒的出现，同时³¹P NMR中诱导出各向同性成分。明确的颗粒被解释为反相胶束，并讨论了心脏毒素分子在这些结构中的定位。
