ISIS Neutron and Muon Source Data Journal

Neutron scattering to characterise protein interactions with solid-liquid interfaces at different densities in bioprocessing

Abstract: Objectives of this proposal aim to shed light on how adsorption processes such as protein A chromatography, used to purify biologics, affect protein propensity for aggregation. Protein A chromatography has been found to increase the aggregation rate of an IgG4 subsequently exposed to low pH. Loading a low concentration of IgG onto the resin increased aggregation rates further. Using neutron reflectivity, we wish to study the conformation of IgG4 when adsorbed to immobilised protein A. We wish to examine whether the conformation or orientation of the adsorbed molecules is affected by either the density of immobilised ligands, or the concentration of protein bound. It is hypothesised that intermolecular forces and rotational freedom affect the structural integrity of the adsorbed proteins, and their orientation in relation to the adsorbent surface, thus influencing aggregation phenomena.

Principal Investigator: Professor Daniel Bracewell
Experimenter: Dr Alice Mazzer
Experimenter: Mr Thomas Johnson
Experimenter: Professor Christopher Roberts
Experimenter: Miss Maria Papachristodoulou
Experimenter: Dr Luke Clifton

DOI: 10.5286/ISIS.E.RB1610150

ISIS Experiment Number: RB1610150

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Professor Daniel Bracewell et al; (2016): Neutron scattering to characterise protein interactions with solid-liquid interfaces at different densities in bioprocessing, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1610150

Data is released under the CC-BY-4.0 license.