Original Air Date: April 24, 2018
Time: On-Demand
Determination of relative abundance of glycoforms is a critical quality attribute for monoclonal antibodies, since different glycosylation patterns affect numerous factors including effector function, pharmacokinetics, clearance, and immunogenicity. With such compound complexity comes the need for even greater resolution between different protein forms as well as methods and technologies that promote greater consistency and address potential protein adsorption issues.
Many existing separation modes and methods are currently employed to characterize and quantitate relative abundance of glycoforms. In this presentation we will build on these tools by focusing on how a combination of optimized LC methods, new particle chemistries (both core-shell and thermally modified fully porous), and new biocompatible LC hardware all combine to initiate greater resolution, better throughput, and more consistent results overall.
Specifically, we will discuss the strengths and limitations of each of the following techniques: intact mass by LC-MS with a high-resolution Q-TOF, HILIC LC-MS of glycopeptides, HILIC LC-MS of released N-linked glycans, and HPLC/UHPLC Size Exclusion.
You will learn about:
- The performance advantages and versatility of 7 new LC particle chemistries spanning RP, HILIC and SEC
- How to minimize the need for column priming
- Differentiated released glycan retention profile provided by unique column stationary phase
Who should attend:
- All scientists or analysts that wish to learn more about the benefits of combining core-shell and fully porous columns for the characterization of glycoforms, while greatly minimizing the need for column priming.