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″.
|Original language||English (US)|
|Number of pages||9|
|State||Published - Jun 2006|
All Science Journal Classification (ASJC) codes
- Mechanics of Materials
- Ceramics and Composites