Antibody-drug conjugates (ADCs) are among the most promising—and analytically demanding—modalities in biopharma today. By combining large, heterogeneous antibodies with chemically labile payloads and linkers, ADCs introduce a level of structural complexity that challenges conventional analytical workflows. It also poses the challenge that the very features you need to measure are often the easiest to lose during analysis.
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Why traditional MS/MS falls short for ADCs and how electron-activated dissociation (EAD) changes the equation
Antibody-drug conjugates (ADCs) are among the most promising—and analytically demanding—modalities in biopharma today. By combining large, heterogeneous antibodies with chemically labile payloads and linkers, ADCs introduce a level of structural complexity that challenges conventional analytical workflows. It also poses the challenge that the very features you need to measure are often the easiest to lose during analysis.
ADC analytics FAQs: Answering the most common questions about ADC characterization
Antibody-drug conjugates (ADCs) have emerged as one of the fastest-growing classes of biotherapeutics, combining the targeting specificity of monoclonal antibodies with the potency of cytotoxic payloads. However, this unique architecture also introduces significant analytical complexity. From drug-to-antibody ratio (DAR) distributions and charge variants to conjugation sites and structural modifications, ADCs present multiple, interconnected sources of heterogeneity that must be understood to ensure product quality and performance.
Using Bio Tool Kit for interpreting peptide MS/MS data obtained using electron activated dissociation (EAD)
Peptide MS/MS spectra obtained using either collision induced dissociation (CID) or electron activated dissociation (EAD) can be analyzed using the Peptide Fragments pane in Bio Tool Kit in SCIEX OS Software. First, open the EAD MS/MS spectrum that you want to...
Peptide fragmentation using electron activated dissociation (EAD)
Most workflows in protein quantification and characterization by mass spectrometry have used collision-induced dissociation (CID). In the CID process, a peptide is selected in the first quadrupole of the instrument (Q1), then accelerated through a collision cell where...
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