Szponarski W, Bolard J
Biochim Biophys Acta. 1987 Feb 26;897(2):229-37. doi: 10.1016/0005-2736(87)90419-6.
The interaction of amphotericin B with isolated human erythrocyte ghosts was monitored by circular dichroism at 37 degrees C and 15 degrees C. Although different, these spectra were not concentration dependent over a concentration range covering the inducement of K+ leakage and hemolysis, which suggests the existence of only one bound amphotericin B species. At 15 degrees C, the spectra indicate that amphotericin B is complexed with membrane cholesterol; the complex formation is saturable but not cooperative. At 37 degrees C new spectra are observed, and their existence is conditioned by the presence of membrane proteins. The binding is cooperative but not saturable. The amphotericin B right side-out vesicles complexation is temperature as well as ionic strength dependent: at high ionic strength it is the same as with ghosts, with the same temperature dependence. At low ionic strength it is characteristic of an interaction with cholesterol, regardless of temperature. In the large unilamellar vesicles reconstituted from the total lipid extracts of erythrocyte membranes, amphotericin B is complexed with cholesterol, regardless of temperature and ionic strength. These results indicate that there are two different modes of amphotericin B complexation with erythrocyte membranes, reversible one in the other, depending on the molecular organization of the membrane and the presence of membrane proteins.
在37摄氏度和15摄氏度下，通过圆二色性监测两性霉素B与分离出的人红细胞膜的相互作用。尽管光谱不同，但在涵盖钾离子泄漏和溶血诱导的浓度范围内，这些光谱并不依赖于浓度，这表明仅存在一种结合的两性霉素B物种。在15摄氏度时，光谱表明两性霉素B与膜胆固醇复合；复合物的形成是可饱和的，但不具有协同性。在37摄氏度时，观察到新的光谱，其存在取决于膜蛋白的存在。结合是协同的，但不饱和。两性霉素B与外翻囊泡的复合作用既依赖于温度，也依赖于离子强度：在高离子强度下，其与红细胞膜的情况相同，具有相同的温度依赖性。在低离子强度下，无论温度如何，其特征都是与胆固醇相互作用。在由红细胞膜总脂质提取物重构的大单层囊泡中，无论温度和离子强度如何，两性霉素B都与胆固醇复合。这些结果表明，两性霉素B与红细胞膜存在两种不同的复合模式，这两种模式相互可逆，取决于膜的分子组织和膜蛋白的存在。
