Bovine Serum Albumin and Fibrinogen Adsorption at the 316L Stainless Steel/Aqueous Interface.
Payagalage, Charanee Galabada
The journal of physical chemistry. B
American Chemical Society (ACS)
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Wood, M., Payagalage, C. G., & Geue, T. (2018). Bovine Serum Albumin and Fibrinogen Adsorption at the 316L Stainless Steel/Aqueous Interface.. The journal of physical chemistry. B, 122 (19), 5057-5065. https://doi.org/10.1021/acs.jpcb.8b01347
The binding of bovine serum albumin (BSA) to a 316L stainless steel surface from a buffer solution has been characterised using neutron reflectometry (NR) and quartz crystal microbalance (QCM) 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 pre-adsorbing BSA on fibrinogen adsorption were examined, firstly by prior physisorption of BSA to the stainless steel surface and secondly by pre-treating the stainless steel with a layer of SDS to render it more hydrophobic. Whilst the pre-adsorption 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 was subsequently flowed through. In contrast, the SDS-treated surface yielded both an increased BSA adsorption and consistently decreased fibrinogen adsorption.
Animals, Cattle, Water, Stainless Steel, Sodium Dodecyl Sulfate, Serum Albumin, Bovine, Fibrinogen, Neutron Diffraction, Adsorption, Surface Properties, Hydrophobic and Hydrophilic Interactions, Quartz Crystal Microbalance Techniques
External DOI: https://doi.org/10.1021/acs.jpcb.8b01347
This record's URL: https://www.repository.cam.ac.uk/handle/1810/275560