Static light scattering study of complex formation between protein and neutral water-soluble polymer.
Static light scattering study of complex formation between protein and neutral water-soluble polymer.
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DOI：
10.1016/j.colsurfb.2006.10.011
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发表时间：
2007-04
期刊：
影响因子：
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通讯作者：
Hiroshi Matsunami;Chiho Fujita;K. Ogawa;E. Kokufuta
中科院分区：
文献类型：
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作者：
Hiroshi Matsunami;Chiho Fujita;K. Ogawa;E. Kokufuta
研究了重均分子量为 1,720,000g/mol 的聚（N-异丙基丙烯酰胺）（PNIPA）与人血清白蛋白（HSA）、卵清蛋白（OVA）和溶菌酶（LYZ）在含有 0.01M 氯化钠并调节至 pH 3 的水介质中形成复合物。通过静态光散射（SLS）检查不同摩尔比（rm）的聚合物-蛋白质混合物。使用我们自己的方法对 SLS 数据进行分析 [Kokufuta 等人，Langmuir 15 (1999) 940； Biomacromolecules 4 (2003) 728]表明所得复合物的分子量小于由两条聚合物链加一种蛋白质组成的互聚物复合物的分子量。这表明在所有研究的聚合物-蛋白质系统中形成了聚合物内复合物。因此，在每个rm我们计算每个聚合物的结合蛋白的数量，其值依次为OVA>HSA>LYZ。将这些结果与每种蛋白质的亲水特性进行比较，这是获得有关蛋白质中疏水性和亲水性片段分布信息的良好工具。很明显，聚合物和蛋白质之间的疏水相互作用在聚合物内复合物的形成中起着重要作用。
Complex formation of poly(N-isopropylacrylamide) (PNIPA) having a weight-average molecular weight of 1,720,000g/mol with human serum albumin (HSA), ovalbumin (OVA) and lysozyme (LYZ) was studied in an aqueous medium containing 0.01M NaCl and adjusted to pH 3. The polymer–protein mixtures at different molar ratios (rm) were examined by static light scattering (SLS). The analysis of SLS data using our own approach [Kokufuta et al., Langmuir 15 (1999) 940; Biomacromolecules 4 (2003) 728] showed that the molecular weight of each resulting complex is smaller than that of the interpolymer complex composed of two polymer chains plus one protein. This indicates the formation of an intrapolymer complex in all the polymer–protein systems studied. Thus, at each rmwe calculated the number of bound proteins per polymer, the value of which was OVA>HSA>LYZ in order. These results were compared with the hydropathy profiles of each protein which are a good tool for obtaining an information about distribution of hydrophobic and hydrophilic segments in a protein. It has become apparent that the hydrophobic interaction between polymer and protein plays an important role in the intrapolymer complex formation.