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

Paper ID Volume ID Publish Year Pages File Format Full-Text
10580 692 2006 9 PDF Available
Title
Interfacial rheology of blood proteins adsorbed to the aqueous-buffer/air interface ☆
Abstract

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′G′ and G″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 ΠLV≡γlvo-γlv rises to a sustained maximum ΠLVmax. Mixing as little as 25 w/v% albumin into IgG at fixed total protein concentration substantially reduces peak G′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′G′and G″G″.

Keywords
Plasma; Serum; Protein adsorption; Air–water interface; Interfacial rheology
First Page Preview
Interfacial rheology of blood proteins adsorbed to the aqueous-buffer/air interface ☆
Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 27, Issue 18, June 2006, Pages 3404–3412
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering