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- W2031973921 abstract "The covalent attachment of Fab‘ fragments of polyclonal anti-human IgG to a polymerizable lipid with a terminal linker group (N-(e-maleimidocaproyl)dilinoleoylphosphatidylethanolamine) was examined by means of quartz crystal microbalance (QCM), surface plasmon resonance (SPR), and atomic force microscopy (AFM). The linker lipid was embedded in a monolayer of dilinoleoylphosphatidylethanolamine. Both monomeric and cross-linked biofunctionalized monolayers were studied. Atomic force microscope images showed that the monomeric monolayer consisted of large holes when it was deposited on a solid substrate, while the cross-linked monolayer appeared as a planar two-dimensional film. The ability of the biofunctionalized monolayer to bind proteins decreased with UV-irradiation time. However, an increase in the linker lipid concentration in the lipid matrix increased the protein-binding efficiency. A comparison between QCM and SPR measurements indicated that the QCM measurements overestimated the binding efficiency..." @default.
- W2031973921 created "2016-06-24" @default.
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- W2031973921 date "2000-05-01" @default.
- W2031973921 modified "2023-10-17" @default.
- W2031973921 title "Protein Immobilization to a Partially Cross-Linked Organic Monolayer" @default.
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- W2031973921 doi "https://doi.org/10.1021/la990817+" @default.
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