Arnaud Delobel | Authors

The methodologies demonstrated here open the way to fully compliant at-line monitoring of monoclonal antibody quality attributes.

Among all the analytical techniques available for epitope mapping studies, hydrogen–deuterium exchange mass spectrometry (HDX-MS) is usually the fastest and easiest to carry out. We present here the epitope mapping of three distinct monoclonal antibody (mAb) candidates targeting the same antigen, an interleukin receptor. The goal is to establish the binding mode of these mAbs, and explain possible differences observed for in vitro binding and in vivo function.

This is the final instalment in a series of four articles exploring topics that will be addressed at the HPLC 2016 conference in San Francisco, USA, from 19–24 June 2016.

High-resolution mass spectrometry (MS) is not readily compatible with chromatographic techniques using high-salt mobile phases. This study presents the development and use of 2D-LC–MS via an on-line desalting step for the analysis of monoclonal antibodies and antibody–drug conjugates.

As a result of advances in multilevel state-of-the-art mass spectrometry (MS) methods, combined with chromatographic and electrophoretic techniques, very precise characterization of biotherapeutics such as monoclonal antibodies (mAbs) and antibody drug conjugates (ADCs) is now possible. Until recently, however, these techniques were considered suitable only for research use. With the advent of robust and user-friendly solutions, these techniques are now amenable for routine use, as illustrated by examples of applications of the characterization of mAbs and ADCs. This is the fourth in a series of four articles exploring topics that will be addressed at the HPLC 2016 conference in San Francisco, from June 19 to 24.