Title:Characterization of Pharmaceutical IgG and Biosimilars Using Miniaturized Platforms and LC-MS/MS
Volume: 17
Issue: 9
Author(s): Kerry M. Wooding, Wenjing Peng and Yehia Mechref
Affiliation:
Keywords:
IgG, microscale immobilized enzyme reactors, chips, IgG, biosimilars, LC-MS.
Abstract: Therapeutic monoclonal antibodies (mAbs) have made a tremendous impact in treating patients
with various diseases. MAbs are designed to specifically target a cell and illicit a response from
the immune system to destroy the cell. As originator mAb drug patents are coming to an end, generic
pharmaceutical companies are poised to replicate and produce so-called biosimilar drugs. MAbs are
significantly more complicated than small drugs to analyze and produce. The mAb proteoform and
glycoform must be as similar to the original drug as possible to be a viable replacement. The mAb proteoform
is well characterized but can be altered through various undesirable reactions such as deamidation.
The mAb glycoform is harder to replicate as the glycan formation is a complicated templateless
one; it is proving difficult for the originator companies to produce a homogenous population of mAbs from batch to
batch. Severe side-effects have occurred in patients taking mAbs with immunogenic glycans, highlighting the importance
of quality control mechanisms. The complex nature of mAbs requires sensitive and robust tools amenable to the highthroughput
analysis required by a manufacturing setting. Miniaturized analytical platforms for complex biosimilar analysis
are still in their infancy but have shown great promise for sample preparation. Capillary electrophoresis-laser induced
fluorescence remains a powerful and fast technique for routine glycan analysis. Mass spectrometry is the method of choice
for the analysis of mAb proteoforms and is emerging as a powerful tool for glycoform analysis.
