ELLIPSOMETRY STUDIES OF PROTEIN LAYERS ADSORBED AT HYDROPHOBIC SURFACES
ELLIPSOMETRY STUDIES OF PROTEIN LAYERS ADSORBED AT HYDROPHOBIC SURFACES
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DOI：
10.1006/jcis.1994.1303
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发表时间：
1994-09-01
影响因子：
9.9
通讯作者：
MALMSTEN, M
中科院分区：
文献类型：
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作者：
MALMSTEN, M
用原位椭圆偏振法研究了人血清白蛋白（HSA）、IgG、纤维蛋白原和溶菌酶等模型蛋白质在甲基化二氧化硅表面的吸附。 通过在两个不同的环境折射率和使用四区平均的裸基板进行研究，吸附量，吸附层厚度，和平均吸附层折射率得到。 获得的蛋白质的吸附量同意与以前的结果。 吸附层的厚度变化强烈的蛋白质之间。 因此，在吸附平台，对于HSA、溶菌酶、IgG和纤维蛋白原获得的吸附层厚度（delta（el））分别为4 +/-2、11 +/-2、18 +/-2和28 +/-2nm。 吸附层的积累进行不同的蛋白质。 因此，对于纤维蛋白原，Δ（el）和吸附层平均折射率（n（f））均单调增加至约4 mg/m2。 另一方面，对于IgG，delta（el）基本上与吸附量无关，而n（f）线性增加。 最后，由溶菌酶形成的吸附层比由纤维蛋白原、IgG和HSA形成的吸附层更致密。 这些发现进行了讨论的吸附层结构。 (C)1994年出版社出版。
The adsorption of some model proteins, human serum albumin (HSA), IgG, fibrinogen, and lysozyme, at methylated silica surfaces was investigated with in situ ellipsometry. By performing studies with the bare substrate at two different ambient refractive indices and using four-zone averaging, the adsorbed amount, the adsorbed layer thickness, and the mean adsorbed layer refractive index are obtained. The adsorbed amounts obtained for the proteins agree well with previous results. The adsorbed layer thicknesses vary strongly between the proteins. Thus, at adsorption plateau, the adsorbed layer thicknesses (delta(el)) obtained for HSA, lysozyme, IgG, and fibrinogen are 4 +/- 2, 11 +/- 2, 18 +/- 2, and 28 +/- 2 nm, respectively. The buildup of the adsorbed layers proceeds differently for different proteins. Thus, for fibrinogen, both delta(el) and the adsorbed layer mean refractive index (n(f)) increase monotonically up to about 4 mg/m2. For IgG, on the other hand, delta(el) is essentially independent of the adsorbed amount, whereas n(f) increases linearly. Finally, the adsorbed layer formed by lysozyme is more compact than those formed by fibrinogen, IgG, and HSA. These findings are discussed in terms of adsorbed layer structure. (C) 1994 Academic Press, Inc.