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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Complex Formation between Bovine Serum Albumin and Strong Polyelectrolytes: Effect of Polymer Charge Density
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Complex Formation between Bovine Serum Albumin and Strong Polyelectrolytes: Effect of Polymer Charge Density

机译：牛血清白蛋白与强聚电解质之间的复合物形成：聚合物电荷密度的影响

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摘要

Light scattering and pH titration were used to examine the binding of bovine serum albumin (BSA (diallyldimethylammonium chloride) (PDADMAC), poly(acrylamidomethylpropyl sulfonate) (PAMPS),poly-(methacrylamidopropyltrimethylammonium chloride) (PMAPTAC), and an AMPS-acrylamide random copolymer (PAMPS↓(80)AAm↓(20)). The critical protein charge required to induce protein-polyelectrolyte complexation, (Zpr)↓(c), was found to vary linearly with the square root of the ionic strength (lin), i.e.with the Debye-Hückel parameter (κ), the proportionality constant being a function of polyelectrolyte chain parameters such as intrinsic stiffness and charge density. This linearity was remarkably continuous through with (Zpr) ↓(c) occurring predominantly "on the wrong side" of the isoionic point; i.e., the onset of binding was typically observed when the global protein charge was of the same sign as the polyelectrolyte. Binding of BSA to the lower charge density polyanion (PAMPS↓(80)Aam↓(20)) unexpectedly occurred under conditions where binding to the more highly charged homopolyanion (PAMPS) did not. The theoretical treatment of Muthukumar was used to interpret the linearity of (Zpr)↓(c) vs I↑(1/2)and the observed influence of polyelectrolyte structural parameters. The apparent applicability of this model to the heterogeneous amphoteric protein surface suggests that binding of polyelectrolytes takes place at "charge patches" whose effective charge densities are from, but nevertheless linearly dependent on, the global charge density.
机译：使用光散射和pH滴定法检测牛血清白蛋白（BSA（二烯丙基二甲基氯化铵）（PDADMAC），聚（丙烯酰胺基甲基丙基磺酸）（PAMPS），聚-（甲基丙烯酰胺基丙基三甲基氯化铵）（PMAPTAC）和AMPS-丙烯酰胺的结合共聚物（PAMPS↓（80）AAm↓（20））。诱导蛋白质-聚电解质络合所需的关键蛋白质电荷（Zpr）↓（c）与离子强度的平方根成线性关系（lin） ，即使用Debye-Hückel参数（κ），比例常数是诸如固有刚度和电荷密度之类的聚电解质链参数的函数。这种线性关系非常明显，其中（Zpr）↓（c）主要出现在“错误的位置”上等离子点的“侧”;即，当总蛋白质电荷与聚电解质具有相同符号时，通常会观察到结合的开始。BSA与较低电荷密度的聚阴离子的结合（PAMPS↓（80）Aam↓（20） ）没想到通常在不与更高电荷的均聚阴离子（PAMPS）结合的条件下发生。 Muthukumar的理论处理用于解释（Zpr）↓（c）与I↑（1/2）的线性关系以及所观察到的聚电解质结构参数的影响。该模型对异质两性蛋白表面的明显适用性表明，聚电解质的结合发生在“电荷斑块”上，其有效电荷密度来自但仍线性依赖于总体电荷密度。

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