Antibody-polysorbate surface interactions

DOI

Of concern to the bioprocessing industry is the manner in which polysorbates included in solution formulations of antibodies affect the kinetics and equilibrium state of antibody adsorption/desorption to hydrophilic (glass) and hydrophobic (plastics) surfaces. Work with MedImmune has investigated this scenario using total internal reflection fluorescence (TIRF), showing that the time taken to reach equilibrium and the final amount of antibody adsorbed is strongly dependent on the shear rate and bulk concentration of antibody and polysorbate. Solid state circular dichroism showed that antibody structure was lost upon adsorption to hydrophobic surfaces. We propose to obtain high resolution data for adsorbed antibody over a range of concentrations in order to interpret kinetic data for antibody adsorption with/without polysorbate acquired over 120 s timescales to fit with the TIRF data.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24088082
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24088082
Provenance
Creator Dr Cameron Neylon; Dr Luke Clifton; Dr Chris van der Walle; Mr Ruairidh Couston; Dr Shahid Uddin; Miss Stephanie Jones; Professor Martin King
Publisher ISIS Neutron and Muon Source
Publication Year 2014
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 Photon- and Neutron Geosciences
Temporal Coverage Begin 2011-10-21T06:29:01Z
Temporal Coverage End 2011-12-17T07:32:11Z