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首页> 外文期刊>Biomacromolecules >pH Dependence and Protein Selectivity of Poly(ethyleneimine)/ Poly(acrylic acid)Multilayers Studied by in Situ ATR-FTIR Spectroscopy
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pH Dependence and Protein Selectivity of Poly(ethyleneimine)/ Poly(acrylic acid)Multilayers Studied by in Situ ATR-FTIR Spectroscopy

机译：原位ATR-FTIR光谱法研究聚乙烯亚胺/聚丙烯酸多层膜的pH依赖性和蛋白质选择性

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The selective interaction between polyelectrolyte multilayers (PEM)consecutively adsorbed from poly-(ethyleneimine)(PEI)and poly(acrylic acid)(PAC)and a binary mixture containing concanavalin A (COA)and lysozyme (LYZ)based on electrostatic interaction is reported.The composition and structure of the PEM and the uptake of proteins were analyzed by in situ attenuated total reflection (ATR)Fourier transform infrared (FTIR)spectroscopy,and the morphology and thickness were characterized by atomic force microscopy (AFM)and ellipsometry.The PEM dissociation degree and charge state and the protein adsorption were shown to be highly dependent on the outermost layer type and the pH in solution.High protein uptake was obtained under electrostatically attractive conditions.This was used to bind selectively one protein from a binary mixture of LYZ/COA.In detail it could be demonstrated that six-layered PEM-6 at pH = 7.3 showed a preferential sorption of positively charged LYZ,while at PEM-5 and pH = 7.3 negatively charged COA could be selectively bound.No protein sorption from the binary mixture was observed at pH = 4.0 for both PEM,when COA,LYZ,and the outermost PEI layer of PEM-5 were positively charged or the outermost PAC layer of PEM-6 was neutral.Furthermore,from factor analysis of the spectral data the higher selectivity was found for PEM-5 compared to PEM-6.Increasing the ionic strength revealed a drastic decrease in the selectivity of both PEM.Evidence was found that the proteins were predominantly bound at the surface and to a minor extent in the bulk phase of PEM.These results suggest possible working regimes and application fields of PEI/PAC multilayer assemblies related to the preparative separation of binary and multicomponent protein mixtures (biofluids,food)as well as to the design of selective protein-resistant surfaces.
机译：报道了通过静电相互作用连续吸附聚（乙烯亚胺）（PEI）和聚（丙烯酸）（PAC）的聚电解质多层膜（PEM）与包含伴刀豆球蛋白A（COA）和溶菌酶（LYZ）的二元混合物之间的选择性相互作用用原位衰减全反射傅里叶变换红外光谱（FTIR）光谱仪分析PEM的组成和结构以及蛋白质的摄取，并通过原子力显微镜（AFM）和椭偏仪表征其形貌和厚度。 PEM的解离度和电荷状态以及蛋白质的吸附高度依赖于最外层的类型和溶液中的pH值，在静电吸引条件下获得了很高的蛋白质吸收率，用于选择性地结合二元混合物中的一种蛋白质LYZ / COA。详细地，可以证明六层PEM-6在pH = 7.3时表现出优先吸附带正电荷的LYZ，而在PEM-5和pH下= 7.3带负电荷的COA可以被选择性结合。当pH = 4.0时，PEM均未观察到二元混合物的蛋白质吸附，当COA，LYZ和PEM-5的最外层PEI层带正电或PAC的最外层PAC层PEM-6是中性的。此外，通过光谱数据的因子分析，发现PEM-5的选择性比PEM-6高。离子强度的增加表明两种PEM的选择性都大大降低。蛋白质主要在PEM的表面上结合，并在较小程度上结合在PEM上。这些结果表明PEI / PAC多层组件的可能的工作方式和应用领域与二元和多组分蛋白质混合物（生物流体，食品）的制备分离有关以及选择性抗蛋白质表面的设计。

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