Katsu T, Kobayashi H, Fujita Y
Biochim Biophys Acta. 1986 Sep 11;860(3):608-19. doi: 10.1016/0005-2736(86)90560-2.
The action of a cationic antibiotic gramicidin S on the outer and cytoplasmic membranes of Escherichia coli was studied. It was found that gramicidin S disrupted the permeability barrier of the outer membrane, permitting the permeation of an antibiotic ionophore, this being similar to the action of the dimer in compound 48/80 (Katsu, T., Shibata, M. and Fujita, Y. (1985) Biochim. Biophys. Acta 818, 61-66). However, differently from the dimer, gramicidin S further stimulated the efflux of K+ through the cytoplasmic membrane of E. coli. The time course of K+ permeability change accorded well with that of change in the viability of E. coli cells. These changes occurred at temperatures above the phase transition of the cytoplasmic membrane. This temperature range differed greatly from the case of polymyxin B, a polycationic antibiotic acting at temperatures above the phase transition of the outer membrane. We discuss the mode of gramicidin S action on the cytoplasmic membrane of E. coli, in comparison with the results on red blood cells and liposomes.
研究了阳离子抗生素短杆菌肽S对大肠杆菌外膜和细胞质膜的作用。发现短杆菌肽S破坏了外膜的通透性屏障,使抗生素离子载体得以渗透,这与化合物48/80中二聚体的作用相似(胜田,T.,柴田,M.和藤田,Y.(1985年)《生物化学与生物物理学报》818,61 - 66)。然而,与二聚体不同的是,短杆菌肽S进一步刺激了钾离子通过大肠杆菌细胞质膜的外流。钾离子通透性变化的时间进程与大肠杆菌细胞活力变化的时间进程吻合良好。这些变化发生在细胞质膜相变温度以上。这个温度范围与多粘菌素B的情况有很大不同,多粘菌素B是一种在高于外膜相变温度下起作用的聚阳离子抗生素。我们将短杆菌肽S对大肠杆菌细胞质膜的作用方式与红细胞和脂质体的研究结果进行了比较。