Competitive Adsorption from Mixed Hen Egg-White Lysozyme/Surfactant Solutions at the Air−Water Interface Studied by Tensiometry, Ellipsometry, and Surface Dilational Rheology

Abstract

The competitive adsorption at the air-water interface from mixed adsorption layers of hen egg-white lysozyme with a non-ionic surfactant (C10DMPO) was studied and compared to the mixture with an ionic surfactant (SDS) using bubble and drop shape analysis tensiometry, ellipsometry, and surface dilational rheology. The set of equilibrium and kinetic data of the mixed solutions is described by a thermodynamic model developed recently. The theoretical description of the mixed system is based on the model parameters for the individual components.

Electrospray–differential mobility analysis of bionanoparticles

“…However, labeling may change the conformation stability of proteins, and affect their adsorption behavior or even promote aggregation in proteins [87,95,96]. To avoid the adverse effects of labeling, other "label-free" tools have been employed such as size exclusion chromatography [87,95,96], electrophoresis [128], ellipsometry [132,133], spectroscopy [134], surface plasmon resonance [101], quartz crystal microbalance [135], tensiometry [132], reflectrometry [136], shear rheology [125], surface force apparatus [137] and imaging techniques [138]. However, there are only a few reports where these tools have been employed on oligomers (monomers, dimers etc) of the same protein [87][88][89].…”

Adsorption of proteins at the solution/air interface influenced by added non-ionic surfactants at very low concentrations for both components. 1. Dodecyl dimethyl phospine oxide

“…The number of bound surfactants per protein molecule depends essentially on the solution pH. The addition of non-ionic surfactants can lead to complexes with proteins probably via hydrophobic interactions and the formation of mixed adsorption layers was described so far mainly by a competitive adsorption mechanism [5][6][7][8]13]. Non-ionic surfactants induce a competitive adsorption phenomenon and lead finally at sufficiently high surfactant concentrations to the replacement of the protein from the interface.…”

Formation of Protein and Protein–Gold Nanoparticle Stabilized Microbubbles by Pressurized Gyration

“…It must be noted that proteins are surface-active molecules and can preferentially adsorb at the water−air interface, 27 and this phenomenon can locally modify the surface tension of the system. Thus, eq 1 in our analysis above may need further modification to include this effect on the surface tension.…”