ArticleFrontiers in pharmacology2014
Assessing analytical methods to monitor isoAsp formation in monoclonal antibodies.
Article in Frontiers in pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 35 citations in OpenAlex.
- In-Depth Characterization for Methionine Oxidization in Complementary Domain Region by Hydrophobic Interaction Chromatography.ACS pharmacology & translational science · 2024Article
- Impact of Excipient Extraction and Buffer Exchange on Recombinant Monoclonal Antibody Stability.Molecular pharmaceutics · 2024Article
- LC-MS Approach to Decipher a Light Chain Chromatographic Peak Splitting of a Monoclonal Antibody.Pharmaceutical research · 2023Article
- Differentiation of Aspartic and Isoaspartic Acid Using 193 nm Ultraviolet Photodissociation Mass Spectrometry.Analytical chemistry · 2023Article
- Pertuzumab Charge Variant Analysis and Complementarity-Determining Region Stability Assessment to Deamidation.Analytical chemistry · 2023Article
- Developability assessment at early-stage discovery to enable development of antibody-derived therapeutics.Antibody therapeutics · 2023Review
- High-Resolution Demultiplexing (HRdm) Ion Mobility Spectrometry-Mass Spectrometry for Aspartic and Isoaspartic Acid Determination and Screening.Analytical chemistry · 2022Article
- Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy.Journal of biomolecular NMR · 2021Article
- Assessing and Improving Protein Sample Quality.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Establishment of a highly precise multi-attribute method for the characterization and quality control of therapeutic monoclonal antibodies.Bioengineered · 2020Article
- A post-translational modification of human Norovirus capsid protein attenuates glycan binding.Nature communications · 2019Article
- Article
- Sequence and Solution Effects on the Prevalence of d-Isomers Produced by Deamidation.ACS chemical biology · 2017Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A ubiquitous post-translational modification observed in proteins is isomerization of aspartic acid to isoaspartic acid (isoAsp). This non-enzymatic post-translational modification occurs spontaneously in proteins and plays a role in aging, autoimmune response, cancer, neurodegeneration, and other diseases. Formation of isoAsp is also a significant issue for recombinant monoclonal antibody based protein therapeutics particularly when isomerization occurs in a complementarity-determining region due to potential impact to the clinical efficacy. Here, we present and compare three analytical methods to monitor and/or quantify isoAsp formation in a monoclonal antibody. The methods include two peptide map based technologies with quantitation from either UV integration or total ion peak areas, as well as an alternative approach using IdeS digestion to generate Fc/2 and Fab'2 regions, followed by hydrophobic interaction chromatography (HIC) to separate the population of Fab'2 containing an isoAsp. The level of isoAsp detected by the peptide map and the digested-HIC methods presented here show similar trends although sample throughput varies by method.
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