Ohmori N, Niidome T, Hatakeyama T, Mihara H, Aoyagi H
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Japan.
J Pept Res. 1998 Feb;51(2):103-9. doi: 10.1111/j.1399-3011.1998.tb00626.x.
To investigate the interaction of amphiphilic alpha-helical peptides with phospholipid membranes, we synthesized Ac-(Leu-Ala-Arg-Leu)3-NHCH3 (4[3]) and three derivatives, in which the chain length and the size of the hydrophobic region of the peptides were different from each other. These peptides formed an alpha-helical structure in the presence of vesicles. In the membrane-perturbation measurement, only 43 showed a strong membrane-perturbation activity below phase-transition temperature (25 degrees C), but above phase-transition temperature (50 degrees C), most peptides showed similar strong activities. On the other hand, in membrane-fusion measurement the long peptides, e.g., Ac-(Leu-Ala-Arg-Leu)3-(Leu-Arg-Ala-Leu)3-NHCH3, had strong activities at low peptide concentrations at 25 degrees C. The present study indicated a parallel relationship did not always exist between membrane fusion and perturbation caused by peptides.
为了研究两亲性α-螺旋肽与磷脂膜的相互作用，我们合成了Ac-(Leu-Ala-Arg-Leu)3-NHCH3（4[3]）及其三种衍生物，这些肽的链长和疏水区域大小各不相同。这些肽在囊泡存在的情况下形成α-螺旋结构。在膜扰动测量中，只有43在相变温度（25℃）以下表现出较强的膜扰动活性，但在相变温度（50℃）以上，大多数肽表现出类似的强活性。另一方面，在膜融合测量中，长肽，例如Ac-(Leu-Ala-Arg-Leu)3-(Leu-Arg-Ala-Leu)3-NHCH3，在25℃下低肽浓度时具有较强活性。本研究表明，肽引起的膜融合和扰动之间并不总是存在平行关系。
