Interfacial rheology of blood proteins adsorbed to the aqueous-buffer/air interface

被引：45
作者：
Ariola, FS
Krishnan, A
Vogler, EA [1 ]
机构：
[1] Penn State Univ, Dept Mat Sci & Engn, Mat Res Inst, Huck Inst Life Sci, University Pk, PA 16802 USA
[2] Penn State Univ, Huck Inst Life Sci, Integrat Biosci Grad Program, University Pk, PA 16802 USA
[3] Penn State Univ, Dept Bioengn, University Pk, PA 16802 USA
来源：
BIOMATERIALS | 2006年 / 27卷 / 18期
关键词：
plasma; serum; protein adsorption; air-water interface; interfacial rheology;
D O I：
10.1016/j.biomaterials.2006.02.005
中图分类号：
R318 [生物医学工程];
学科分类号：
0831 ;
摘要：
Concentration-dependent, interfacial-shear rheology and interfacial tension of albumin, IgG, fibrinogen, and IgM adsorbed to the aqueous-buffer/air surface is interpreted in terms of a single viscoelastic layer for albumin but multi-layers for the larger proteins. Two-dimensional (2D) storage and loss moduli G' and G '', respectively, rise and fall as a function of bulk-solution concentration, signaling formation of a network of interacting protein molecules at the surface with viscoelastic properties. Over the same concentration range, interfacial spreading pressure Pi(LV) gamma degrees(lv) - gamma(lv) rises to a sustained maximum Pi(max)(LV). Mixing as little as 25 w/v% albumin into IgG at fixed total protein concentration substantially reduces peak G', strongly suggesting that albumin acts as rheological modifier by intercalating with adsorbed IgG molecules. By contrast to purified-protein solutions, serially diluted human blood serum shows no resolvable concentration-dependent G' and G ''. (c) 2006 Elsevier Ltd. All rights reserved.
引用
收藏
页码：3404 / 3412
页数：9
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