Structure of biodegradable films at aqueous surfaces: X-ray diffraction and spectroscopy studies of polylactides and tyrosine-derived polycarbonates.
Structure of biodegradable films at aqueous surfaces: X-ray diffraction and spectroscopy studies of polylactides and tyrosine-derived polycarbonates.
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水表面可生物降解薄膜的结构：聚丙交酯和酪氨酸衍生的聚碳酸酯的 X 射线衍射和光谱研究。
DOI：
10.1021/la401268s
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Vaknin,David
中科院分区：
文献类型：
--
作者：
Wang,Wenjie;Murthy,NSanjeeva;Kuzmenko,Ivan;Anderson,NathanielA;Vaknin,David
采用表面压力-面积等温线（Π-A）和表面敏感x射线衍射技术对三种具有增加模量代表性的聚合物聚（d，l-乳酸）、PDLLA、聚（去氨基酪氨酸-酪氨酸乙酯酯）、PDTEC以及具有碘化DTE片段的相同聚合物PI2DTEC进行了表征。通过在空气-水界面铺展稀释聚合物溶液，制备了10-100 Å厚度的薄膜。等温线的一般性质和Flory指数分别随PDLLA、PDTEC、PI2DTEC模量的增加而变化。对水表面薄膜的原位x射线反射率和掠射x射线衍射（GIXD）测量结果的分析提供了与聚合物模量一致的形态图，并且在很大程度上与它们在干散货状态下的包装一致。碘对x射线的大量吸收使近全反射条件下的x射线光谱研究能够确定PI2DTEC薄膜中的碘分布，并补充由反射率和GIXD得出的结构模型。这些结构研究为今后研究聚合物-蛋白质在水界面的相互作用奠定了基础。
Three representative polymers of increasing modulus, poly(d,l-lactic acid), PDLLA, poly(desaminotyrosyl-tyrosine ethyl ester carbonate), PDTEC, and the same polymer with iodinated DTE segments, PI2DTEC, were characterized by surface-pressure versus area (Π–A) isotherms and surface sensitive X-ray diffraction techniques. Films of 10–100 Å thickness were prepared for these studies by spreading dilute polymer solutions at air–water interfaces. The general properties of the isotherms and the Flory exponents, determined from the isotherms, vary in accordance with the increasing modulus of PDLLA, PDTEC, PI2DTEC, respectively. The analysis of in situ X-ray reflectivity and grazing incidence X-ray diffraction (GIXD) measurements from films at aqueous surfaces provides a morphological picture that is consistent with the modulus of the polymers, and to a large extent, with their packing in their dry-bulk state. Large absorption of X-rays by iodine enabled X-ray spectroscopic studies under near-total-reflection conditions to determine the iodine distribution in the PI2DTEC film and complement the structural model derived from reflectivity and GIXD. These structural studies lay the foundation for future studies of polymer–protein interactions at aqueous interfaces.
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