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

DOI

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.

Identifier
DOI https://doi.org/10.5286/ISIS.E.87814866
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/87814866
Provenance
Creator Professor Stephen Perkins; Dr James Doutch; Miss Hina Iqbal; Ms Gar Kay Hui; Miss Valentina Spiteri
Publisher ISIS Neutron and Muon Source
Publication Year 2020
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2017-10-05T08:00:00Z
Temporal Coverage End 2017-10-11T07:24:24Z