Different interactions of egg-yolk phosphatidylcholine and sphingomyelin with detergent bile salts.

To examine physical-chemical aspects of bile salt-phospholipid interactions that could contribute to preferential phosphatidylcholine (PC) secretion into bile, we have compared transitions between vesicles and micelles in model systems containing taurocholate (TC) and either egg-yolk PC (EYPC), egg-yolk sphingomyelin (EYSM), buttermilk SM (BMSM) or dipalmitoyl PC (DPPC). Phase transitions from micelles to vesicles were observed at 4-fold dilution of serially diluted EYPC/TC systems, but not earlier than at 16-fold dilution of SM/TC or DPPC/TC systems, indicating lower concentrations of the detergent required for micellization in the case of SM or DPPC. Cryo-transmission electron microscopy of phase transitions initiated by addition of TC to phospholipid vesicles revealed extremely long SM-containing intermediate structures, but shorter EYPC-containing intermediate structures. Again, larger amounts of bile salt were required to induce phase transitions in the case of EYPC compared to SM. Sizes of TC-phospholipid micelles increased progressively upon increasing phospholipid contents in the rank order: DPPC-TC<EYSM-TC<BMSM-TC<EYPC-TC, consistent with higher micellization concentrations in the case of EYPC. Micelles were also separated from vesicular phases in two-phase model systems composed with TC, both EYPC and EYSM and 0, 10, 20 or 30 mol% cholesterol, by ultracentrifugation and ultrafiltration of the supernatant. At increasing cholesterol contents, EYPC preferentially distributed into the micellar phase. In contrast, no preferential micellar EYPC distribution occurred in the absence of the sterol. These results indicate different structural arrangements of EYPC-TC micelles compared to SM-TC micelles and lower detergent concentrations required for micellization in the case of SM-containing vesicles.