Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118, USA.
J Phys Chem B. 2010 Mar 11;114(9):3276-84. doi: 10.1021/jp908730t.
Phospholipid monolayers play a critical role in the structure and stabilization of biological interfaces, including all membranes, the alveoli of the lungs, fat droplets in adipose tissue, and lipoproteins. The behavior of phospholipids in bilayers and at an air-water interface is well understood. However, the study of phospholipids at oil-water interfaces is limited due to technical challenges. In this study, egg phosphatidylcholine (EPC) was deposited from small unilamellar vesicles onto a bubble of either air or triolein (TO) formed in a low-salt buffer. The surface tension (gamma) was measured using a drop tensiometer. We observed that EPC binds irreversibly to both interfaces and at equilibrium exerts approximately 12 and 15 mN/m of pressure (Pi) at an air and TO interface, respectively. After EPC was bound to the interface, the unbound EPC was washed out of the cuvette, and the surface was compressed to study the Pi/area relationship. To determine the surface concentration (Gamma), which cannot be measured directly, compression isotherms from a Langmuir trough and drop tensiometer were compared. The air-water interfaces had identical characteristics using both techniques; thus, Gamma on the bubble can be determined by overlaying the two isotherms. Both TO and EPC are surface-active, so in a mixed TO/EPC monolayer, both molecules will be exposed to water. Since TO is less surface-active than EPC, as Pi increases, the TO is progressively ejected. To understand the Pi/area isotherm of EPC on a TO bubble, a variety of TO-EPC mixtures were spread at the air-water interface. The isotherms show an abrupt break in the curve caused by the ejection of TO from the monolayer into a new bulk phase. By overlaying the compression isotherm above the ejection point with a TO bubble compression isotherm, Gamma can be estimated. This allows determination of Gamma of EPC on a TO bubble as a function of Pi.
磷脂单层在生物界面的结构和稳定中起着关键作用,包括所有的膜、肺的肺泡、脂肪组织中的脂肪滴和脂蛋白。磷脂在双层和气-水界面的行为已经得到很好的理解。然而,由于技术挑战,磷脂在油-水界面的研究受到限制。在这项研究中,从小单层囊泡中沉积的卵磷酯(EPC)在低盐缓冲液中形成的空气或三油酸甘油酯(TO)泡上。使用滴形张力计测量表面张力(γ)。我们观察到 EPC 不可逆地结合到两个界面上,在平衡状态下,在空气和 TO 界面上分别施加约 12 和 15 mN/m 的压力(Pi)。EPC 结合到界面后,将未结合的 EPC 从比色杯中洗出,并压缩表面以研究 Pi/面积关系。为了确定无法直接测量的表面浓度(Γ),比较了来自 Langmuir 槽和滴形张力计的压缩等温线。两种技术的空气-水界面具有相同的特性;因此,可以通过叠加两个等温线来确定气泡上的 Γ。TO 和 EPC 都是表面活性剂,因此在 TO/EPC 混合单层中,两种分子都将暴露在水中。由于 TO 比 EPC 的表面活性低,随着 Pi 的增加,TO 会逐渐被排出。为了理解 TO 气泡上 EPC 的 Pi/面积等温线,在空气-水界面上展开了各种 TO-EPC 混合物。等温线显示出曲线的突然中断,这是由于 TO 从单层中排出到新的体相引起的。通过将超过排出点的压缩等温线与 TO 气泡压缩等温线重叠,可以估计 Γ。这允许根据 Pi 确定 TO 气泡上 EPC 的 Γ。