Effect of electrostatic interaction on the adsorption of globular proteins on octacalcium phosphate crystal film.
Effect of electrostatic interaction on the adsorption of globular proteins on octacalcium phosphate crystal film.
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DOI：
10.1006/jcis.2001.8026
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发表时间：
2002-02
影响因子：
9.9
通讯作者：
Woo-Kul Lee;J. Ko;Hyun-Man Kim
中科院分区：
文献类型：
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作者：
Woo-Kul Lee;J. Ko;Hyun-Man Kim
研究了静电对球形蛋白质如牛血清白蛋白(BSA)、蛋清溶菌酶(LZM)和β-乳球蛋白(β-LG)在类八钙磷酸钙(OCP)晶体薄膜上吸附的影响。在组织培养聚苯乙烯(TCP)表面合成了一种结晶度较差的薄膜，并将其作为模型表面。溶液的pH明显影响蛋白质和表面的静电性质。在准稳定状态下获得的吸附量很容易与每种蛋白质的溶液pH相关。吸附速率在初始阶段较快，然后逐渐趋于平稳。BSA和LZM的最大吸附质量分别出现在pH 7和pH 9。当p Hs低于9时，β-lg吸附相同的量，但当p Hs大于9时，存在静电斥力时，吸附质量减小。出现最大吸附质量的pH值可以认为是静电吸引最有利的条件。在目的蛋白中，β-LG的吸附质量最大，而BSA的吸附最小，尽管它的分子质量较大。LZM属于中间区域。根据这些观察，BSA发生了构象变化，在更大程度上阻止了进一步的吸附。吸附速率与静电性能之间没有建立简单的关系。然而，初始阶段的吸附速率的数量级趋于与每个蛋白质的最大吸附质量的数量级相同。
The electrostatic effect on the adsorption of globular proteins, such as bovine serum albumin (BSA), hen egg white lysozyme (LZM), and beta-lactoglobulin (beta-Lg), on octacalcium phosphate (OCP)-like crystal thin films was investigated. A poorly crystalline thin film was synthesized on a tissue culture polystyrene (TCP) surface and used as a model surface in this study. The solution pH clearly affected the electrostatic properties of both proteins and surface. The adsorbed amounts obtained at quasi-steady state were readily related to the solution pH for each protein. The adsorption rate is fast during the initial period and levels off gradually. The maximum adsorbed mass occurred at pH 7 for BSA and at pH 9 for LZM. beta-Lg adsorbed similar amounts at pHs lower than 9, but the adsorbed mass decreased at pHs higher than 9 where electrostatic repulsion exists. The pH values where the maximum adsorbed mass occurred may be considered as the conditions where electrostatic attraction is most favorable. The adsorbed mass of beta-Lg was the greatest among the proteins of interest while BSA adsorbed the least despite its greater molecular mass. LZM falls into the intermediate region. According to these observations, BSA has undergone conformational changes that prevent further adsorption to a greater extent than the others. A simple relationship between the adsorption rate and the electrostatic properties was not established. However, the order of magnitude of the adsorption rate at the initial period tends to be the same as that of maximum adsorbed mass for each protein.