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Updated: Feb 11, 2026

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
Published on: April 9, 2017
Asparagine Deamidation in a Complementarity Determining Region of a Recombinant Monoclonal Antibody in Complex with
Christine Nowak1, Ashish Tiwari1, Hongcheng Liu1
1Product Characterization , Alexion Pharmaceuticals , 100 College Street , New Haven , Connecticut 06510 , United States.
Abstract:
Asparagine deamidation in the complementarity determining regions of recombinant monoclonal antibodies has been extensively studied and shown to have a negative impact on antigen binding. Those asparagine residues are typically exposed and thus have a higher tendency toward deamidation, depending also on local structure and environmental factors such as temperature and pH. Deamidation rates and products of a susceptible asparagine residue in the complementarity determining regions of a recombinant monoclonal antibody free in solution or in the antibody-antigen complex were studied. The results demonstrated that incubation of the antibody or its antigen complex generated a similar amount of aspartate. The expected amount of isoaspartate product was detected in free antibody, but it was completely lacking in the antibody-antigen complex.
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