Matsuzaki K, Murase O, Fujii N, Miyajima K
Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Biochemistry. 1995 May 16;34(19):6521-6. doi: 10.1021/bi00019a033.
A channel-forming antimicrobial peptide, magainin 2, has been shown to translocate across phospholipid bilayers by forming a pore comprising multimeric peptides. The translocation was demonstrated by four sets of experiments by use of resonance energy transfer from tryptophan introduced into the peptide to a dansyl chromophore incorporated into the lipid membrane. The translocation was coupled to pore formation, as detected by the dye efflux from the lipid vesicles; about 30% of the total peptide molecules translocated into the inner leaflets over 10 min, while 80% of the dye molecules leaked out at a lipid to peptide ratio of 57. This novel model can explain the problems debated so far, i.e., the peptide forms an ion channel whereas the magainin helix essentially lies parallel to the membrane surface. Channel (pore) formation in the vesicles is a transient process observable mainly during the early stage of the peptide membrane interactions.
一种形成通道的抗菌肽，蛙皮素2，已被证明可通过形成由多聚体肽组成的孔道穿过磷脂双层膜。通过四组实验证明了这种转运，实验利用了从引入肽中的色氨酸到掺入脂质膜中的丹磺酰发色团的共振能量转移。这种转运与孔道形成相关联，这可通过脂质囊泡中的染料外排检测到；在10分钟内，约30%的总肽分子转运到内小叶，而在脂质与肽的比例为57时，80%的染料分子泄漏出去。这个新模型可以解释迄今为止所争论的问题，即肽形成离子通道，而蛙皮素螺旋基本上与膜表面平行。囊泡中通道（孔道）的形成是一个主要在肽与膜相互作用的早期阶段可观察到的短暂过程。
