Desorption of fibrinogen and γ-globulin from solid surfaces induced by a nonionic detergent

doi:10.1016/0021-9797(89)90407-4

Journal of Colloid and Interface Science

Volume 128, Issue 1, 1 March 1989, Pages 296-300

https://doi.org/10.1016/0021-9797(89)90407-4 Get rights and content

Abstract

The action of a nonionic detergent (Tween 20) on adsorbed layers of fibrinogen or γ-globulin on solid surfaces was studied. The solid surface used was a hydrophilic silicon dioxide surface with a gradient of hydrophobic methyl groups (wettability gradient surface). The amount of adsorbed organic material on the gradient surface was determined with the use of an optical method (ellipsometry) with sufficiently high lateral resolution. It was demonstrated that Tween 20 has a small effect on desorption of adsorbed proteins on the hydrophilic side of the gradient. Desorption of proteins occurred, however, at the hydrophobic side of the gradient. Desorption of the protein layers was strongly inhibited by incubation of the adsorbed protein layers in buffer at 37°C for 4 h before incubation in Tween 20. A probable explanation for this is that the adsorbed protein molecules gradually increase their hydrophobic interaction with the surface during the incubation time.

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This observation is different from the previous report by Dixit et al.11 in which QCM result showed no desorption of the preadsorbed Fc-fusion protein when polysorbate 20 was introduced in their system. Therefore, the ability of a surfactant to displace surface-adsorbed protein appears to be dependent on the binding affinity for the specific protein versus the surfactant.41,42 Presumably, the strong interaction between a hydrophobic silicone oil surface and nonionic surfactant results in competitive displacement of adsorbed protein molecules at the interface.
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Gradient surfaces are the one that displays a gradual change in its chemical and physical properties along their length [1]. The earliest research on gradient wettability surfaces was seen in 1855 [2], and from then on, gradient wettability surfaces, with a water contact angle gradually change along their length, have attracted extensive interests for fundamental researches and practical applications because of their potential applications in a wide variety of fields such as protein absorption [3–6], cell adhesion [7,8], microfluidics fabrication [9–13], and heat transfer enhancement in heating/cooling systems [1(a),14,15]. To fabricate gradient wettability surfaces, typical procedures are to create chemical composition gradient, surface roughness gradient, or chemical composition gradient with surface roughness gradient.
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This observation is consistent with previous results on hydrophobic interfaces for different surfactants (Joshi and McGuire, 2009; Liu and Kim, 2009). However, studies on surfaces of varying wettability showed Tween® desorption when rinsed with buffer, suggesting its reversibility (Elwing et al., 1989). Resistance or dissipation denotes the viscous contribution to the total frequency shift and represents the energy loss associated with adsorption.
There is evidence in the literature that silicone oil, a lubricant, can induce aggregation in protein formulations delivered through prefilled syringes. Surfactants are commonly used to minimize protein–silicone oil and protein–container interactions; however, these interactions are not well characterized and understood. The purpose of this manuscript was to understand the competitive interactions of a fusion protein with the silicone oil in the presence of Tween^® 20. An adsorption isotherm for Tween^® 20 at the silicone oil/water interface, using silicone oil coated quartz crystals, was generated at 25 °C to identify surface saturation concentrations. A concentration of Tween^® 20 providing interfacial saturation was selected for protein adsorption studies at the silicone oil/water interface. The surfactant molecules adsorbed at the interface in a monolayer with a reduced viscoelastic character in comparison to the bound protein layer. A significant reduction in protein adsorption was observed when the surfactant was present at the interface. No desorption of the pre-adsorbed protein molecules was observed when Tween^® 20 was introduced, suggesting that the protein has strong interactions with the interface. However, both, Tween^® 20 and protein, adsorbed to the silicone oil/water interface when adsorption was carried out from a mixture of protein and Tween^® 20.
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In particular, when introduced to an adsorbed protein layer on a hydrophilic surface, nonionic surfactants generally have little effect on the adsorbed amount. In contrast, on hydrophobic surfaces, nonionic surfactants typically have a substantial effect on the adsorbed protein, presumably because of the difference in surfactant binding strength at the interface [49]. Joshi and McGuire [50] have described the interaction of lysozyme, a well-characterized globular protein, with the nonionic surfactant polysorbate 80 at solid-water interfaces.
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NoteDesorption of fibrinogen and γ-globulin from solid surfaces induced by a nonionic detergent

Abstract

J. Colloid Interface Sci.

J. Colloid Interface Sci.

J. Colloid Interface Sci.

J. Colloid Interface Sci.

J. Immunol. Methods

J. Non-Cryst. Solids

J. Colloid Interface Sci.

J. Colloid Interface Sci.

J. Colloid Interface Sci.

J. Colloid Interface Sci.

Eur. J. Biochem.

J. Chem. Soc. Faraday Trans.

FEMS Microbiol. Ecol.

Note
Desorption of fibrinogen and γ-globulin from solid surfaces induced by a nonionic detergent