Effects of polyethylene glycol on protein interactions
Effects of polyethylene glycol on protein interactions
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DOI：
10.1063/1.1321042
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发表时间：
2000-12-01
影响因子：
4.4
通讯作者：
Zukoski, CF
中科院分区：
文献类型：
--
作者：
Kulkarni, AM;Chatterjee, AP;Zukoski, CF
通过测量蛋白质溶液第二维里系数 (B-2) 来探究聚乙二醇 (PEG) 存在下球状蛋白质之间的相互作用。PEG 的溶液特性以四种分子量（400、1000、6000 和 12000）为特征，为 B-2 的测量和理论预测进行定量比较提供了机会。PEG 显示了缓冲液和分子量依赖性的较低临界溶液温度。随着聚合物溶液接近相分离，耗尽吸引力的后果显着增加。对于含有 PEG 的硫酸盐缓冲液中的溶菌酶和牛血清白蛋白，标准消耗模型无法很好地描述 B-2。这种失败在醋酸盐缓冲液中更加严重，其中 B-2 是聚合物浓度的非单调函数。 B-2 中有吸引力的最小值与 PEG 水溶液的加热诱导相分离密切相关。消耗相互作用的热聚合物参考相互作用位点模型很好地捕获了两种蛋白质在 PEG 存在下的实验数据，其中聚合物密度波动相关长度被视为温度、聚合物浓度和分子量的函数。 (C) 2000 年美国物理研究所。 [S0021-9606(00)50245-1]。
The interactions between globular proteins in the presence of poly (ethylene glycol) (PEG) are probed through the measurement of the protein solution second virial coefficient (B-2) The solution properties of PEG are characterized for four molecular weights (400, 1000, 6000, and 12 000), providing an opportunity for quantitative comparison of measurements and theoretical predictions of B-2 PEG displays a buffer and molecular weight-dependent lower critical solution temperature. As the polymer solution approaches phase separation, the consequences of depletion attractions increase significantly. For lysozyme and bovine serum albumin in sulfate buffers with PEG, B-2 is not well described by standard depletion models. This failure is accentuated in acetate buffers where B-2 is a nonmonotonic function of polymer concentration. The attractive minima in B-2 are closely associated with the proximity of the heating-induced phase separation of aqueous PEG solutions. The experimental data for both proteins in the presence of PEG are well captured by the thermal polymer reference interaction site model for depletion interactions where the polymer density fluctuation correlation length is treated as a function of temperature, polymer concentration, and molecular weight. (C) 2000 American Institute of Physics. [S0021-9606(00)50245-1].