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Bovine Serum Albumin and Fibrinogen Adsorption at the 316L Stainless Steel/Aqueous Interface.

Accepted version
Peer-reviewed

Type

Article

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Authors

Payagalage, Charanee Galabada 
Geue, Thomas 

Abstract

The binding of bovine serum albumin (BSA) to a 316L stainless steel surface from a buffer solution has been characterized using neutron reflectometry and quartz crystal microbalance measurements; coverage at all concentrations up to a near-physiological concentration was found to be relatively low (<20%); the protein followed a two-step isotherm adsorption model type and the overall thickness at the higher concentrations (around 80 Å) suggested possible multilayering and/or protein unfolding. As it has been postulated that BSA may inhibit the further adsorption of another blood plasma protein-fibrinogen-the effects of preadsorbing BSA on fibrinogen adsorption were examined, first by prior physisorption of BSA to the stainless steel surface and second by pretreating the stainless steel with a layer of sodium dodecyl sulfate (SDS) to render it more hydrophobic. Although the preadsorption of BSA to an untreated stainless steel surface did slightly decrease the amount of fibrinogen adsorbed initially, it had no inhibiting effect if a solution containing solely fibrinogen subsequently flowed through. In contrast, the SDS-treated surface yielded both an increased BSA adsorption and consistently decreased fibrinogen adsorption.

Description

Keywords

Adsorption, Animals, Cattle, Fibrinogen, Hydrophobic and Hydrophilic Interactions, Neutron Diffraction, Quartz Crystal Microbalance Techniques, Serum Albumin, Bovine, Sodium Dodecyl Sulfate, Stainless Steel, Surface Properties, Water

Journal Title

J Phys Chem B

Conference Name

Journal ISSN

1520-6106
1520-5207

Volume Title

122

Publisher

American Chemical Society (ACS)