Recombinant monoclonal antibody (mAb) therapeutics constitute a large segment of the biologics market as they have shown success in many therapeutic areas. N-linked glycosylation on the Fc- portion of mAbs is a common post-translational modification that can have a significant impact on the mAbs therapeutic efficacy, in vivo half-life, and safety. As a result, N-linked glycan composition is considered a critical quality attribute and the glycoform profile is required for mAb characterization. Current methodologies to assess glycosylation involve complex techniques that couple extensive separation methods with mass spectrometry or nuclear magnetic resonance spectroscopy. Although these techniques provide detailed structural information about the mAb’s glycosylation state, they can be costly and require extensive time and significant expertise. For process screening and monitoring (e.g., bioreactor and downstream process vessels), such complex structural information may not be required. Instead, analytical technologies that indicate levels of product and it’s glycosylation state may be sufficient, particularly when coupled with data analytic methods that provide discrimination and model-based control schemes. To meet this measurement need, we developed an electrochemical based interface that is rapidly electroassembled onto electrodes and when linked with glycan-recognizing lectins reveals levels of mAbs with the appropriate terminal glycan moieties. Further, when coupled with a protein G:HRP reporter this interface enables process control ready electrochemical output. Further, a new thiolated protein-G construct enables total mAb titre. That is, our interface is rapidly constructed using electrode actuated redox reactions enabling hydrogel assembly from thiolated-polyethylene glycol (PEG). Then, thiolated sugar groups (e.g., galactose) and sugar-specific lectins are layered on top of the PEG hydrogel. These surfaces then provide selective capture of mAbs based on the traditional lectin-mAb binding. Our glycosensing approach is advantageous as it is simple, portable, inexpensive and can provide fast, quantifiable results for bioprocessing applications.

Simple, rapidly assembled saccharide-based sensor interface that enables interrogation of antibody glycosylation and titer for improved process analytical technologies

Macromolecular Chemistry: The Second Century

[Author Benefits](https://scimeetings.acs.org/?utm_source=pubs_content_marketing&utm_medium=website&utm_campaign=0320_MCF_NPI_Launch_Spring_Homepage&ref=pubs_content_marketing)

[How to use SciMeetings](https://storage.googleapis.com/dl.morressier.com/acs/SciMeetings-ACSSpring2020-HowToGuide_M3020-Final.pdf)

[Frequently Asked Questions](https://storage.googleapis.com/dl.morressier.com/acs/SciMtng_ACSNMSp2020_FAQ_M3120_Final.pdf)

ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.