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

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

Research output: Contribution to journalArticlepeer-review

43 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≡γlvolv 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″.

Original languageEnglish (US)
Pages (from-to)3404-3412
Number of pages9
JournalBiomaterials
Volume27
Issue number18
DOIs
StatePublished - Jun 1 2006

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Ceramics and Composites
  • Biophysics
  • Biomaterials
  • Mechanics of Materials

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