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Antibody adsorption on the surface of water studied by neutron reflection.

ABSTRACT: Surface and interfacial adsorption of antibody molecules could cause structural unfolding and desorbed molecules could trigger solution aggregation, resulting in the compromise of physical stability. Although antibody adsorption is important and its relevance to many mechanistic processes has been proposed, few techniques can offer direct structural information about antibody adsorption under different conditions. The main aim of this study was to demonstrate the power of neutron reflection to unravel the amount and structural conformation of the adsorbed antibody layers at the air/water interface with and without surfactant, using a monoclonal antibody 'COE-3' as the model. By selecting isotopic contrasts from different ratios of H2O and D2O, the adsorbed amount, thickness and extent of the immersion of the antibody layer could be determined unambiguously. Upon mixing with the commonly-used non-ionic surfactant Polysorbate 80 (Tween 80), the surfactant in the mixed layer could be distinguished from antibody by using both hydrogenated and deuterated surfactants. Neutron reflection measurements from the co-adsorbed layers in null reflecting water revealed that, although the surfactant started to remove antibody from the surface at 1/100 critical micelle concentration (CMC) of the surfactant, complete removal was not achieved until above 1/10 CMC. The neutron study also revealed that antibody molecules retained their globular structure when either adsorbed by themselves or co-adsorbed with the surfactant under the conditions studied.

SUBMITTER: Smith C

PROVIDER: S-EPMC5384797 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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Antibody adsorption on the surface of water studied by neutron reflection.

Smith Charles C Li Zongyi Z Holman Robert R Pan Fang F Campbell Richard A RA Campana Mario M Li Peixun P Webster John R P JR Bishop Steven S Narwal Rojaramani R Uddin Shahid S van der Walle Christopher F CF Lu Jian R JR

mAbs 20170210 3

Surface and interfacial adsorption of antibody molecules could cause structural unfolding and desorbed molecules could trigger solution aggregation, resulting in the compromise of physical stability. Although antibody adsorption is important and its relevance to many mechanistic processes has been proposed, few techniques can offer direct structural information about antibody adsorption under different conditions. The main aim of this study was to demonstrate the power of neutron reflection to u ...[more]

PMID: 28353420

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Project description:Water dynamics in inorganic nanotubes is studied by neutron scattering technique. Two types of aluminosilicate nanotubes are investigated: one is completely hydrophilic on the external and internal surfaces (IMO-OH) while the second possesses an internal cavity which is hydrophobic due to the replacement of Si-OH bonds by Si-CH3 ones (IMO-CH3), the external surface being still hydrophilic. The samples have internal radii equal to 7.5 and 9.8 Å, respectively. By working under well-defined relative humidity (RH) values, water dynamics in IMO-OH was revealed by quasi-elastic spectra as a function of the filling of the interior of the tubes. When one water monolayer is present on the inner surface of the tube, water molecules can jump between neighboring Si-OH sites on the circumference by 2.7 Å. A self-diffusion is then measured with a value (D = 1.4 × 10-5 cm2 s-1) around half of that in bulk water. When water molecules start filling also the interior of the tubes, a strong confinement effect is observed, with a confinement diameter (6 Å) of the same order of magnitude as the radius of the nanotube (7.5 Å). When IMO-OH is filled with water, the H-bond network is very rigid, and water molecules are immobile on the timescale of the experiment. For IMO-OH and IMO-CH3, motions of the hydroxyl groups are also evidenced. The associated relaxation time is of the order of 0.5 ps and is due to hindered rotations of these groups. In the case of IMO-CH3, quasi-elastic spectra and elastic scans are dominated by the motions of methyl groups, making the effect of the water content on the evolution of the signals negligible. It was however possible to describe torsions of methyl groups, with a corresponding rotational relaxation time of 2.6 ps. The understanding of the peculiar behavior of water inside inorganic nanotubes has implications in research areas such as nanoreactors. In particular, the locking of motions inside IMO-OH when it is filled with water prevents its use under these conditions as a nanoreactor, while the interior of the IMO-CH3 cavity is certainly a favorable place for confined chemical reactions to take place.

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Antibody adsorption on the surface of water studied by neutron reflection.

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Antibody adsorption on the surface of water studied by neutron reflection.

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