ADSORPTION OF COMPLEX PROTEINS AT INTERFACES

ADSORPTION OF COMPLEX PROTEINS AT INTERFACES
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DOI:
10.1351/pac199264111777
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发表时间:
1992-11-01
影响因子:
1.8
通讯作者:
WEI, AP
WEI, AP
中科院分区:
化学4区
文献类型:
--
作者:
ANDRADE, JD;HLADY, V;WEI, AP

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我们之前已经表明,通过仔细考虑蛋白质的三维结构及其稳定性,可以定量地了解模型蛋白质在模型界面的吸附。利用计算机分子图形、动态表面张力、荧光探针和标记以及溶液变性数据,我们可以将蛋白质的化学和结构特性与其界面行为联系起来。我们开发了一种新颖的方法来在简单的径向图(“Tatra”图)中呈现这些数据和相关性。我们现在将这些方法扩展到复杂的多结构域蛋白质。白蛋白由静电性质、电荷-pH 特性和变性方面存在差异的三个大结构域组成。白蛋白的界面活性至少部分归因于其组成域的界面活性。考虑各个域的结构和界面活性可以开发新的、更精确的假设,从而可以设计新的、更好的实验。这些假设允许人们评估和比较吸附数据,包括动力学和等温线、吸附层厚度、折射率、多层形成等。我们强烈地感觉到,每种不同的蛋白质都是独特的分子个性,如果我们要更全面地理解和应用复杂蛋白质的界面行为,就必须理解和考虑这一点。参考文献 1-4 提供了对这些主题的扩展处理。
We have previously shown that the adsorption of model proteins at model interfaces can be quantitatively understood via a careful consideration of the proteins' three dimensional structure and its stability. Using computer molecular graphics, dynamic surface tension, fluorescence probes and labels, and solution denaturation data, we can relate the chemical and structural properties of proteins to their interface behavior. We have developed a novel means to present these data and correlations in a simple radial plot (the "Tatra" plot). We are now extending these approaches to complex multi-domain proteins. Albumin consists of three large domains with differences in electrostatic nature, charge-pH characteristics, and denaturability. The interfacial activity of albumin is due, at least in part, to the interfacial activity of its constituent domains. Consideration of the structure and interfacial activity of the various domains permits new and more precise hypotheses to be developed, with which new and better experiments can be designed. Such hypotheses allow one to evaluate and compare adsorption data, including kinetics and isotherms, adsorbed layer thickness, refractive index, multilayer formation, etc. We feel strongly that each different protein is a unique molecular personality, which must be understood and considered if we are to more fully understand and apply the interfacial behavior of complex proteins. Expanded treatments of these topics are available in References 1-4.