Separation Of A GLP-1 Receptor Agonist And Structurally Similar Impurities Using BioResolve™ Peptide Phenyl‑Hexyl+ And C18+ Columns

By Hua Yang and Steve Shiner

GLP-1 therapeutics are reshaping the biopharmaceutical market, but their peptide-based structures bring complex analytical challenges across development, manufacturing, and storage. Even small structural changes, including deamidation, isoaspartate formation, single amino acid D-enantiomers, or amino acid substitutions, can affect product quality and require confident separation and characterization. For tirzepatide, these closely related impurities can be difficult to resolve using standard approaches. By comparing BioResolve Peptide Phenyl-Hexyl+ and BioResolve Peptide C18+ RP Columns, scientists can see how column chemistry influences selectivity and enables separation of structurally similar peptide impurities.

Access the full application note to explore how targeted column selection can support impurity profiling strategies for complex GLP-1 therapeutics.