Organization of Albumin on Polymer Surfaces

Eberhart, Robert C.; Munro, M. S.; Frautschi, Jack R.; Севастьянов, В. И.

doi:10.1021/bk-1987-0343.ch024

Cited by 17 publications

(14 citation statements)

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“…This thinking is consistent with the facts that unlike the other proteins, both BSA adsorption kinetic (16) and adsorption equilibrium behavior (30) have been observed to be similar at hydrophobic and hydrophilic silica surfaces. Moreover, human serum albumin shows great homology with BSA and is known to passivate biomedical material surfaces to fibrinogen adsorption and platelet adhesion (8). In fact, retention of albumin on blood-contacting implants to reduce thrombogenesis remains a major focus in biomedical materials research (13).…”

Section: Surface These Hydrophobicmentioning

confidence: 99%

Influence of preadsorbed milk proteins on adhesion of Listeria monocytogenes to hydrophobic and hydrophilic silica surfaces

Al-Makhlafi

McGuire

Daeschel

1994

Appl Environ Microbiol

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The adsorption of 13-lactoglobulin, bovine serum albumin, a-lactalbumin, and jI-casein for 8 h and P-lactoglobulin and bovine serum albumin for 1 h at silanized silica surfaces of low and high hydrophobicity, followed by incubation in buffer and contact with Listeria monocytogenes, resulted in different numbers of cells adhered per unit of surface area. Adhesion to both surfaces was greatest when jI-lactoglobulin was present and was lowest when bovine serum albumin was present. Preadsorption of ot-lactalbumin and 13-casein showed an intermediate effect on cell adhesion. Adsorption of P-lactoglobulin for 1 h resulted in a generally lower number of cells adhered compared with the 8-h adsorption time, while the opposite result was observed with respect to bovine serum albumin. The adhesion data were explainable in terms of the relative rates of arrival to the surface and postadsorptive conformational change among the proteins, in addition to the extent of surface coverage in each case.

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Section: Surface These Hydrophobicmentioning

confidence: 99%

Influence of preadsorbed milk proteins on adhesion of Listeria monocytogenes to hydrophobic and hydrophilic silica surfaces

Al-Makhlafi

McGuire

Daeschel

1994

Appl Environ Microbiol

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“…By attaching alkyl chains to polymer surfaces by various methods, researchers have been able to increase surface affinity toward albumin. [6][7][8] It has also been reported that as the length of the grafted alkyl chain increases from 2 to 18 carbon atoms, the albumin desorption rate decreases. 9 The interaction between albumin and an alkylated surface is affected not only by alkyl chain length.…”

Section: Introductionmentioning

confidence: 96%

“…Therefore, alkylation of surfaces has been used as a pathway to increase the surface binding of albumin. By attaching alkyl chains to polymer surfaces by various methods, researchers have been able to increase surface affinity toward albumin. − It has also been reported that as the length of the grafted alkyl chain increases from 2 to 18 carbon atoms, the albumin desorption rate decreases …”

Section: Introductionmentioning

confidence: 99%

Atomic Force Microscopy and X-ray Reflectivity Studies of Albumin Adsorbed onto Self-Assembled Monolayers of Hexadecyltrichlorosilane

et al. 1998

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Atomic force microscopy (AFM) and X-ray reflectivity (XR) have been used together to provide a detailed and direct look at the structure of human serum albumin protein adsorbed onto well-characterized selfassembled monolayer (SAM) surfaces at several protein concentrations. The duration of SAM deposition was also varied to investigate the influence of the density of hydrocarbon chains in the SAM on protein binding tenacity. Concurrent study of adsorption to bare silicon wafers with native oxide surfaces provided a comparison with a hydrophilic surface similar to widely studied glass and quartz surfaces. Both AFM and XR measurements showed that after adsorption, rinsing, and drying, the surfaces of all substrates were covered with no more than a single layer of adsorbed protein. Thin dense protein layers were seen for the substrates exposed to protein concentrations of 0.1 and 0.5 mg/mL. Partial surface coverage by protein aggregates having larger thicknesses was seen for substrates exposed to lower concentrations. The tenacity of the protein adsorption on different substrates was tested by eluting the adsorbed protein with a 1% solution of sodium dodecyl sulfate surfactant. This treatment removed almost all protein from the bare silicon surface and from the fully formed, dense SAMs. A significant amount of adsorbed protein remained on the surface of the less dense, "incomplete" monolayers, suggesting that protein adsorbed more tenaciously on that surface.

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“…These methodologies have provided a wealth of macroscopic information reflecting behavior averaged over the entire surface. The structure of single FG proteins and the architecture of FG films have also been probed at microscopic length scales in scanning electron microscopy (SEM) investigations. Recently, immunogold labeling combined with SEM imaging has been utilized to probe the architecture of adsorbed FG films .…”

Section: Introductionmentioning

confidence: 99%

“…For example, platelet adhesion correlates with factors other than the total amount of FG adsorbed, suggesting that the orientation of the adsorbed FG is significant 12c, and the concentration of FG in solution before adsorption. 15c, There is also evidence for postadsorptive transitions in the FG structure, which highlights the complexity of FG interfacial interactions. Common methods employed to probe the conformation of FG in adsorbed films are generally indirect, involving observation of the protein's ability to bind platelets 14,17a and antibodies 14a,d,17a,18 or measuring the amount of protein that is eluted from the surface by a surfactant such as sodium dodecyl sulfate (SDS). , Spectroscopic techniques such as infrared spectroscopy 7 and circular dichroism have also been utilized to probe conformational changes in protein layers.…”

Section: Introductionmentioning

confidence: 99%

Real-Time Observation of Plasma Protein Film Formation on Well-Defined Surfaces with Scanning Force Microscopy

1998

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We report here the results of a scanning force microscopic (SFM) investigation into the structure of adsorbed bovine fibrinogen films on well-defined surfaces. SFM images show that a monolayer of fibrinogen assembles on both highly oriented pyrolytic graphite (HOPG) and mica. We find, however, that the film morphology varies as a function of the substrate. To unravel the nature of the observed differences, we tracked the growth of bovine fibrinogen layers at both surfaces in real-time. Consistent with the differences observed in the final film structure, we find that film formation on HOPG and mica proceeds through distinct mechanisms. A network is observed during fibrinogen film formation on HOPG, implying that protein−protein interactions are involved in the growth mechanism and likely govern the final film structure. The growth mechanism on mica proceeds by the homogeneous increase in the number of nuclei across the surface and gives no indication of significant intermolecular interactions. Surfactant elution studies show that films on HOPG are more tightly bound than those on mica, as predicted on the basis of the observed growth mechanisms. An adsorption mechanism consistent with our observations and based on the known structure of fibrinogen is proposed.

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Organization of Albumin on Polymer Surfaces

Cited by 17 publications

References 0 publications

Influence of preadsorbed milk proteins on adhesion of Listeria monocytogenes to hydrophobic and hydrophilic silica surfaces

Influence of preadsorbed milk proteins on adhesion of Listeria monocytogenes to hydrophobic and hydrophilic silica surfaces

Atomic Force Microscopy and X-ray Reflectivity Studies of Albumin Adsorbed onto Self-Assembled Monolayers of Hexadecyltrichlorosilane

Real-Time Observation of Plasma Protein Film Formation on Well-Defined Surfaces with Scanning Force Microscopy

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