Equilibrium adsorption of human serum albumin and human fibrinogen on hydrophobic and hydrophilic surfaces

Brynda, Eduard; Cepalova, N. A.; Štol, M.

doi:10.1002/jbm.820180609

Cited by 65 publications

(28 citation statements)

References 14 publications

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“…The amounts of BSA adsorbed to the different substrata were similar and in the range 0.1-1.0 pg cm-2 as reported by Hlady et al (1986), Brynda et al (1984, Horbett (1982) and Brash & Samak (1978). The BSA coating resulted in smaller differences of ys between the substrata, although in the case of FEP an influence of the low substratum free energy was still evident.…”

Section: Discussionsupporting

confidence: 85%

Adhesion of Oral Streptococci from a Flowing Suspension to Uncoated and Albumin-coated Surfaces

Pratt-Terpstra

Weerkamp²,

Busscher³

1987

Microbiology

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A flow cell system was developed which allowed the study of bacterial adhesion to solid substrata at well-defined shear rates. In addition, the system enabled the solid surfaces to be coated with a proteinaceous film under exactly the same shear conditions. In this flow cell system, adhesion of three strains of oral streptococci from a phosphate-buffered solution onto three different substrata was studied as a function of time in the absence and presence of a bovine serum albumin (BSA) coating at a shear rate of 21 s-'. To obtain a wide range in surface free energies (y) representative strains (Yb 38-1 17 mJ m-2) and solid substrata (y, 20-109 mJ m-') were selected. The number of bacteria adhering was counted microscopically. In the absence of a BSA coating a linear relation was found between the number of bacteria adhering at saturation (nb.,) and the calculated interfacial free energy of adhesion (AFadh) for each of the three strains. In the presence of a BSA coating the number of bacteria adhering was greatly decreased in all cases. However, despite the presence of the BSA coating there was still a linear relation between the number of bacteria adhering at saturation and the interfacial free energy of adhesion, calculated on the basis of the surface free energy of the uncoated substrata. It can be concluded that the bare, uncoated substratum still influenced bacterial adhesion in spite of the marked influence of a BSA coating.

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Section: Discussionsupporting

confidence: 85%

Adhesion of Oral Streptococci from a Flowing Suspension to Uncoated and Albumin-coated Surfaces

Pratt-Terpstra

Weerkamp²,

Busscher³

1987

Microbiology

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“…Multi-layering of proteins with MW >50 kDa is consistent with previous-reported depletion results [32], interfacial energetics of protein adsorption [23,26,31], and interfacial rheology of blood proteins [36]. Adsorption-competition data presented herein thus supports the conclusion drawn by a number of investigators using a variety of experimental methods over the last twenty years or so [17,[26][27][28][36][37][38][39][40][41][42][43][44][45] that large proteins can, in fact, adsorb from concentrated solutions in multiple layers. Fig.…”

Section: Theoretical Interpretation Of Competitive Adsorptionsupporting

confidence: 90%

“…This surface-saturation idea is not too different from the 'jamming limit' imposed by random-sequential adsorption (RSA) theories which maximizes monolayer adsorption (2D) coverage at about 55% [35,55,56], except that theory embraced by this work explicitly considers adsorption in 3D with a packing efficiency ε [26] (ε ≈ 45% for the aqueous-buffer/air surface) and permits multi-layer adsorption. This view seems more consistent with the large partial-specific volume ν o occupied by protein and the fact that multi-layering of protein that has been experimentally verified in a number of studies [17,[26][27][28][36][37][38][39][40][41][42][43][44][45].…”

Section: Mass Balance For Protein Adsorption Competition Protein Adsosupporting

confidence: 67%

Volumetric interpretation of protein adsorption: Competition from mixtures and the Vroman effect

2007

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A Vroman-like exchange of different proteins adsorbing from a concentrated mixture to the same hydrophobic adsorbent surface is shown to arise naturally from the selective pressure imposed by a fixed interfacial-concentration capacity (w/v, mg/mL) for which protein molecules compete. A size (molecular weight, MW) discrimination results because fewer large proteins are required to accumulate an interfacial w/v concentration equal to smaller proteins. Hence, the surface region becomes dominated by smaller proteins on a number-or-mole basis through a purely-physical process that is essentially unrelated to protein biochemistry. Under certain conditions, this size discrimination can be amplified by the natural variation in protein-adsorption avidity (quantified by partition coefficients P) because smaller proteins (MW <50 kDa) have been found to exhibit characteristicallyhigher P than larger proteins (MW >50kDa). The standard depletion method is implemented to measure protein-adsorption competition between two different test proteins (i and j) for the same hydrophobic octyl sepharose adsorbent particles. SDS-gel electrophoresis is used as a multiplexing, separation-and-quantification tool for this purpose. Identical results obtained using sequential and simultaneous competition of human immunoglobulin G (IgG, protein j) with human serum albumin (HSA, protein i) demonstrates that HSA was not irreversibly adsorbed to octyl sepharose over a broad range of competing solution concentrations. A clearly-observed exchange of HSA for IgG or fibrinogen (Fib) shows that adsorption of different proteins (i competing with j) to the same hydrophobic surface is coupled whereas adsorption among identical proteins (i or j adsorbing from purified solution) is not coupled. Interpretive theory shows that this adsorption coupling is due to competition for the fixed surface capacity. Theory is extended to hypothetical ternary mixtures using a computational experiment that illustrates the profound impact size-discrimination has on adsorption from complex mixtures such as blood.

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“…1), the area of mineral occupied by albumin was estimated to be 0.8 mg/m2 crystallite sur face area. packed, end-on adsorption of BSA would be equiva lent to ~8 mg/m: [Brynda et al, 1984;Soderquist and Walton, 1980], we conclude that BSA on this apatitic material is either not closely packed, or that it is not adsorbed end-on, or that albumin molecules cannot reach every area that is accessible to the small mole cules that are used in a BET analysis.…”

Section: Quantitative Aspectsmentioning

confidence: 99%

Albumin Interaction with Caries-Like Lesions in Bovine Enamel

Linden¹,

Booij²,

Bosch³

et al. 1989

Caries Res

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The exposure of bovine enamel to an albumin-containing demineralizing solution results in penetration of protein into the porous enamel. Washing of this albumin-containing enamel results in a complete (low pretreatment albumin concentrations) or partial removal of the albumin (pretreatment concentrations ≧200 μg/ml^-1). Subsequent exposure to increasing salt concentrations of fluoride, phosphate, calcium or chloride shows a partial removal of albumin at fluoride or phosphate concentrations of 75 mM while complete removal occurred at 150–200 mM fluoride or phosphate. Exposure to either calcium or chloride, even at 3 M concentrations, showed a negligible albumin release. It is proposed that protein removed at high fluoride or phosphate concentrations is bound by a strong interaction between protein-carboxyl groups and calcium on the surface of the enamel mineral. The partial removal of albumin released at low fluoride or phosphate concentrations indicates an enamel-albumin interaction by means of Ca-bridging between protein-carboxyl groups and mineral phosphates. Finally, it is suggested that salt-free washing removes albumin that has lost its native form upon binding to the partially dissolved crystallites of the enamel. It is concluded that enamel is mainly protected from demineralization by the inhibitory effects of protein penetrated into the pores, in addition to possible protection by the pellicle on the surface.

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Equilibrium adsorption of human serum albumin and human fibrinogen on hydrophobic and hydrophilic surfaces

Cited by 65 publications

References 14 publications

Adhesion of Oral Streptococci from a Flowing Suspension to Uncoated and Albumin-coated Surfaces

Adhesion of Oral Streptococci from a Flowing Suspension to Uncoated and Albumin-coated Surfaces

Volumetric interpretation of protein adsorption: Competition from mixtures and the Vroman effect

Albumin Interaction with Caries-Like Lesions in Bovine Enamel

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