Matsuzaki K, Yoneyama S, Miyajima K
Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Biophys J. 1997 Aug;73(2):831-8. doi: 10.1016/S0006-3495(97)78115-3.
Melittin, a bee venom, is a basic amphiphilic peptide, which mainly acts on the lipid matrix of membranes, lysing various cells. To elucidate the molecular mechanism, we investigated its interactions with phospholipid vesicles. The peptide formed a pore with a short lifetime in the membrane, as revealed by the release of an anionic fluorescent dye, calcein, from the liposomes. Our new double-labeling method clarified that the pore size increased with the peptide-to-lipid ratio. Upon the disintegration of the pore, a fraction of the peptides translocated across the bilayer. The pore formation was coupled with the translocation, which was proved by three fluorescence experiments recently developed by our laboratory. A novel model for the melittin pore formation was discussed in comparison with other pore-forming peptides.
蜂毒肽是一种蜂毒，是一种碱性两亲肽，主要作用于细胞膜的脂质基质，使各种细胞溶解。为了阐明其分子机制，我们研究了它与磷脂囊泡的相互作用。如阴离子荧光染料钙黄绿素从脂质体中释放所显示的那样，该肽在膜中形成了寿命较短的孔。我们新的双标记方法表明，孔径随着肽与脂质的比例增加而增大。孔解体后，一部分肽跨双层转运。孔的形成与转运相关联，这已被我们实验室最近开发的三个荧光实验所证实。与其他成孔肽相比，讨论了一种蜂毒肽成孔的新模型。
