Identification of N‐terminal modification for recombinant monoclonal antibody light chain using partial reduction and quadrupole time‐of‐flight mass spectrometry

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Abstract

Since most recombinant monoclonal antibodies (mAbs) contain glutamic acid or glutamate at their N-terminus, cyclization of these residues to form pyroglutamate is an important degradation pathway that often occurs in therapeutic mAb development. In this work, a rapid method was developed to determine pyroglutamate at the N-terminus of mAb light chain by liquid chromatography coupled with electrospray ionization on a quadrupole time-of-flight mass spectrometer (QTOF). High levels of pyroglutamate were found at the N-terminus of the light chain of a typical recombinant mAb. The quantitative results were comparable to those obtained with a more conventional peptide mapping method. The direct method outlined here can be used to evaluate the impact of N-terminal cyclization during the processing of recombinant mAbs.

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