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

Florly S. Ariola; Anandi Krishnan; Erwin A. Vogler

doi:10.1016/j.biomaterials.2006.02.005

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

Florly S. Ariola, Anandi Krishnan, Erwin A. Vogler

Research output: Contribution to journal › Article › peer-review

52 Scopus citations

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′ 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 Π _LV≡γ_lv^o-γ_lv rises to a sustained maximum Π_LV^max. 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″.

Original language	English (US)
Pages (from-to)	3404-3412
Number of pages	9
Journal	Biomaterials
Volume	27
Issue number	18
DOIs	https://doi.org/10.1016/j.biomaterials.2006.02.005
State	Published - Jun 2006

All Science Journal Classification (ASJC) codes

Biophysics
Bioengineering
Ceramics and Composites
Biomaterials
Mechanics of Materials

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10.1016/j.biomaterials.2006.02.005

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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′ 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 Π LV≡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′, 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″.",

author = "Ariola, {Florly S.} and Anandi Krishnan and Vogler, {Erwin A.}",

note = "Funding Information: This work was supported, in part, by the National Institute of Health PHS 5 R01 HL 69965-04, by Johnson &Johnson through the Focused Giving Grant Program, and a grant with the Pennsylvania Department of Health. The Department Pennsylvania Department of Health specifically disclaims responsibility for any analyses, interpretations or conclusions. Authors appreciate additional support from the Huck Institutes of Life Sciences, Materials Research Institute, and Department of Materials Science and Engineering, Penn State University. Authors are indebted to Ms. Carole Hickey for the gift of the CIR-100 and technical advice. The new supplier for the CIR-100 is First Ten Angstroms Europe, Inc. ",

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N2 - 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 Π LV≡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′, 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″.

AB - 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 Π LV≡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′, 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″.

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

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