ISIS Neutron and Muon Source Data Journal

Unravelling the solution structures and stability of industrially-important antibodies with and without glycans

Abstract: The glycosylation of glycoproteins is a major determinant of their stability, and glycans also affect their aggregatibility (precipitation). An understanding of this is essential for improving manufacturing processes. Our extensive background in glycosylation and scattering (see below) indicates that we are ideally positioned to investigate antibody glycan structures in detail. We will compare both glycosylated and deglycosylated IgG antibodies using a combination of neutron and X-ray scattering, ultracentrifugation and modelling. The two overall aims of this project are to (i) identify how the solution properties of glycans affect antibody manufacture and (ii) develop a pipeline of new methods for the rapid atomistic modelling of antibody conformations based on neutron and X-ray scattering fits in order to evaluate the manufacturability of variously glycosylated antibodies.

Principal Investigator: Professor Stephen Perkins
Local Contact: Dr James Doutch
Experimenter: Miss Hina Iqbal
Experimenter: Ms Gar Kay Hui
Experimenter: Miss Valentina Spiteri

DOI: 10.5286/ISIS.E.RB1720358

ISIS Experiment Number: RB1720358

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 Stephen Perkins et al; (2017): Unravelling the solution structures and stability of industrially-important antibodies with and without glycans , STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1720358

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