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• W2014283595 abstract "We have investigated the morphology and surface forces of protein A adsorbed on mica surface in the protein solutions of various concentrations. The force-distance curves, measured with a surface force apparatus (SFA), were interpreted in terms of two different regimens: a large-distance regimen in which an electrostatic double-layer force dominates, and an adsorbed layer regimen in which a force of steric origin dominates. To further clarify the forces of steric origin, the surface morphology of the adsorbed protein layer was investigated with an atomic force microscope (AFM) because the steric repulsive forces are strongly affected by the adsorption mode of protein A molecules on mica. At lower protein concentrations (2 ppm, 10 ppm), protein A molecules were adsorbed side-on parallel to the mica surfaces, forming a monolayer of approximately 2.5 nm. AFM images at higher concentrations (30 ppm, 100 ppm) showed protruding structures over the monolayer, which revealed that the adsorbed protein A molecules had one end oriented into the solution, with the remainder of each molecule adsorbed side-on to the mica surface. These extending ends of protein A overlapped each other and formed a quasi-double layer over the mica surface. These AFM images proved the existence of a monolayer of protein A molecules at low concentrations and a quasi-double layer with occasional protrusions at high concentrations, which were consistent with the adsorption mode observed in the force-distance curves." @default.
• W2014283595 created "2016-06-24" @default.
• W2014283595 creator A5045822635 @default.
• W2014283595 creator A5060039977 @default.
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• W2014283595 date "1998-01-01" @default.
• W2014283595 modified "2023-10-16" @default.
• W2014283595 title "Correlation between Surface Morphology and Surface Forces of Protein A Adsorbed on Mica" @default.
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• W2014283595 doi "https://doi.org/10.1016/s0006-3495(98)77803-8" @default.
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