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首页> 外文会议>Laser Techniques for Condensed-Phase and Biological Systems >Direct observation of phase and morphology changes induced by lung surfactant protein SP-B in lipid monolayers via fluorescence polarized fluorescence Brewster angle and atomic force microscopies
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Direct observation of phase and morphology changes induced by lung surfactant protein SP-B in lipid monolayers via fluorescence polarized fluorescence Brewster angle and atomic force microscopies

机译：通过荧光偏振荧光布鲁斯特角和原子力显微镜直接观察脂质单层中肺表面活性剂蛋白SP-B诱导的相和形态变化

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Abstract: Both human lung surfactant protein SP-B and its amino terminus alter the phase behavior of palmitic acid (PA) monolayers by inhibiting the formation of condensed phases and creating a new fluid PA-protein phase. This phase increase the compressibility of the monolayers by forming a network that separates condensed phase domains at coexistence and persists to high surface pressures. The network changes the monolayer collapse nucleation from a heterogenous to a more homogenous process through isolating individual condensed phase domains. This results in higher surface pressures at collapse, and monolayers easier to respread on expansion, factors essential to the in vivo function of lung surfactant. The network is stabilized by low line tension between the coexisting phases are confirmed by the formation of extended linear domains or 'stripe' phases. Similar stripes are found in monolayers of fluorescein-labeled amino terminus, suggesting that the reduction n line tension is due to the protein. Comparison of isotherm data and observed morphologies of monolayers containing amino terminus with those containing amino terminus with those containing the full length SP-B protein shows that the peptide retains most of the native activity of the protein, which may lead to cheaper and more effective synthetic replacement formulations. !41
机译：摘要：人肺表面活性剂蛋白SP-B及其氨基末端均通过抑制缩合相的形成并创建新的液态PA蛋白相来改变棕榈酸（PA）单层的相行为。该相通过形成在共存时将缩合相域分开并持续承受高表面压力的网络，从而增加了单层的可压缩性。该网络通过隔离各个凝聚相域，将单层塌陷成核过程从异质过程变为异质过程。这导致塌陷时较高的表面压力，并且单层更容易在膨胀时重新扩散，这是肺表面活性剂体内功能必不可少的因素。共存相之间的低线张力使网络稳定，这是通过扩展线性域或“条带”相的形成来确认的。在荧光素标记的氨基末端单层中发现了类似的条纹，这表明n线张力的降低是由于蛋白质引起的。比较等温线数据和观察到的含氨基末端的单层与含氨基末端的单层与包含全长SP-B蛋白的单层的形态，表明该肽保留了该蛋白质的大部分天然活性，这可能导致合成更便宜且更有效替代配方。 ！41

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