Adsorption of ovalbumin modified with stearyl groups on hydrophobic silica

Magdassi, Shlomo; Leibler, David; Braun, Sergei

doi:10.1021/la00092a015

Cited by 12 publications

(2 citation statements)

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“…The affinity of the proteins for hydrophobic surfaces also increased after hydrophobization, and more compact surface layers were formed. This was reported for the adsorption of IgG onto polystyrene latex beads, phosphatidyl choline coated silica, and oil−water emulsion droplets stabilized by egg phospholipids, for adsorption of glucose oxidase onto polystyrene and lipid-coated silica, and for adsorption of ovalbumin on hydrophobic silica …”

Section: Introductionmentioning

confidence: 74%

Adsorption of Native and Hydrophobized Human IgG onto Silica: Isotherms, Calorimetry, and Biological Activity

et al. 2001

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Adsorption onto silica of native human IgG and its hydrophobized forms prepared by covalent attachment of 11, 25, and 52 C8 alkyl chains was studied. All hydrophobized IgGs spontaneously form micellelike aggregates (nanoclusters) in aqueous solutions with a mean diameter of 40 ± 2 nm. Adsorption isotherms are of a high affinity type. The plateau surface concentration of the isotherms depends on the degree of the protein modification, increasing for 11C8−IgG and 25C8−IgG and decreasing for 52C8−IgG as compared with the native protein. The isothermal enthalpies of adsorption for the native and modified IgGs at all degrees of silica surface coverage were found to be endothermic, that is, the adsorption process is entropically driven. For the native IgG, the adsorption isotherm is apparently reversible, while the isotherms for the modified forms display distinct hysteresis. The biological (immunological) activity of the desorbed molecules was evaluated, and it was found that all forms of IgG which were desorbed from silica display reduced ability to react with a specific antibody, goat antihuman IgG, compared to the corresponding forms before adsorption. The immunoassay on desorbed IgGs indicated that hydrophobic modification of the molecule reduced structural alterations observed on adsorption of the native IgG. The decrease in activity was much less pronounced in the range of surface coverage close to the plateau values. Possible mechanisms of adsorption of the hydrophobized forms of IgG are discussed.

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Section: Introductionmentioning

confidence: 74%

Adsorption of Native and Hydrophobized Human IgG onto Silica: Isotherms, Calorimetry, and Biological Activity

et al. 2001

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“…The affinity of the proteins for hydrophobic surfaces also increased after hydrophobization, and more compact monolayers were formed. This was reported for the adsorption of human IgG onto polystyrene latex beads (6) and oil/water emulsion droplets stabilized by egg phospholipids (14), for adsorption of ovalbumin onto hydrophobized silica (15) and for adsorption of human IgG and gelatin A onto phosphatidyl choline-coated silica (16).…”

Section: Introductionmentioning

confidence: 77%