A novel method of determination of protein stability.

Journal of parenteral science and technology : a publication of the Parenteral Drug Association Pub Date : 1992-09-01

D J Burgess, J K Yoon, N O Sahin

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Abstract

A novel method of determination of protein stability is described, which involves interfacial shear rheology of adsorbed protein layers. This technique provides information on the structural-mechanical properties of the adsorbed protein layers which can be related to: the rate of interfacial adsorption, interfacial interactions, and conformational changes in the adsorbed layers. The interfacial shear rheology of the blood proteins, bovine serum albumin and human immunoglobulin G was investigated. The air/aqueous and oil/aqueous interfaces were studied and the interfacial rheological activity of BSA was shown to be similar at three hydrophobic interfaces: air, squalene and mineral oil. The kinetics of interfacial film formation was shown to be time dependent, and aging effects were detected in both interfacial and bulk molecules. The absolute interfacial elasticity values decreased as the temperature increased. The protein solutions exhibited no interfacial rheological activity in the presence of the small surfactant molecules, Tween 80 and lecithin, under the conditions studied.

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一种测定蛋白质稳定性的新方法。

描述了一种新的测定蛋白质稳定性的方法，该方法涉及吸附蛋白质层的界面剪切流变学。该技术提供了吸附蛋白层的结构-力学性能信息，这些信息与:界面吸附速率、界面相互作用和吸附层的构象变化有关。研究了血蛋白、牛血清白蛋白和人免疫球蛋白G的界面剪切流变性。对空气/水界面和油/水界面进行了研究，结果表明，牛血清白蛋白在空气、角鲨烯和矿物油三种疏水界面上的界面流变活性相似。界面膜形成的动力学表现为时间依赖性，并且在界面分子和体分子中都检测到老化效应。界面绝对弹性值随温度升高而减小。在实验条件下，在小表面活性剂t80和卵磷脂的存在下，蛋白质溶液没有界面流变活性。

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Journal of parenteral science and technology : a publication of the Parenteral Drug Association

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