ArticlemAbs
Native size-exclusion chromatography-mass spectrometry: suitability for antibody-drug conjugate drug-to-antibody ratio quantitation across a range of chemotypes and drug-loading levels.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Global publication productivity and research trends on recurrent ovarian cancer: a bibliometric study.Frontiers in oncology · 2024Pooled it
- Advancements in Dual-Load Antibody-Drug Conjugates and Challenges with Quality Analysis.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Formulation Matters: The Overlooked Engine of Stability and Success in Antibody-Drug Conjugates.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Native Taylor/Non-Taylor Dispersion-Mass Spectrometry (TNT-MS) Allows Rapid Protein Desalting and Multiplexed, Label-Free Ligand Screening.Small methods · 2026Article
- New Frontiers in ADC Analysis: Advances in Chromatography, Electrophoresis, and Mass Spectrometry.The AAPS journal · 2025Review
- Analytical strategies for identification and quantitation of heterodimers in co-formulated monoclonal antibody cocktails by native SEC-MS.Scientific reports · 2025Article
- Antibody-Drug Conjugate Stability Probed by Variable-Temperature Electrospray Ionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025Review
- Enhanced Payload Localization in Antibody-Drug Conjugates Using a Middle-Down Mass Spectrometry Approach with Proton Transfer Charge Reduction.Analytical chemistry · 2024Article
- Enhanced Characterization of Lysine-Linked Antibody Drug Conjugates Enabled by Middle-Down Mass Spectrometry and Higher-Energy Collisional Dissociation-Triggered Electron-Transfer/Higher-Energy Collisional Dissociation and Ultraviolet Photodissociation.Antibodies (Basel, Switzerland) · 2024Article
- Antibody-Drug Conjugate Overview: a State-of-the-art Manufacturing Process and Control Strategy.Pharmaceutical research · 2024Review
- Kinetic models towards an enhanced understanding of diverse ADC conjugation reactions.Frontiers in bioengineering and biotechnology · 2024Article
- Antibody drug conjugates as targeted cancer therapy: past development, present challenges and future opportunities.Archives of pharmacal research · 2023Review
- New Technologies Bloom Together for Bettering Cancer Drug Conjugates.Pharmacological reviews · 2022Review
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- Studying protein structure and function by native separation-mass spectrometry.Nature reviews. Chemistry · 2022Review
- Rapid Analysis of Biotherapeutics Using Protein A Chromatography Coupled to Orbitrap Mass Spectrometry.Analytical chemistry · 2021Article
- Native Structural and Functional Proteoform Characterization of the Prolyl-Alanyl-Specific Endoprotease EndoPro fromJournal of proteome research · 2021Review
- State-of-the-Art Native Mass Spectrometry and Ion Mobility Methods to Monitor Homogeneous Site-Specific Antibody-Drug Conjugates Synthesis.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Clinical Pharmacology of Antibody-Drug Conjugates.Antibodies (Basel, Switzerland) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Native size-exclusion chromatography-mass spectrometry (nSEC-MS) is an analytical methodology that is appropriate for accurately quantitating the drug-to-antibody ratio (DAR) on a wide variety of interchain cysteine-linked antibody-drug conjugates (ADCs), irrespective of chemotype. In the current preclinical environment, novel ADCs conjugated with unique drug-linkers need to progress toward the clinic as quickly as possible. Platform analytical approaches can reduce time-to-clinic because key process development and optimization activities can be decoupled from the development of bespoke, molecule-specific analytical methods. In this work, we assessed the potential of nSEC-MS as a platformable, quantitative DAR method. The nSEC-MS method was evaluated according to performance characteristics and parameters described in the ICH guideline Validation of Analytical Procedures: Text and Methodology Q2(R1). In order to comprehensively assess the accuracy and bias of nSEC-MS DAR quantitation, ADCs were generated using three different drug-linker chemotypes with DARs ranging from 2 to 8. These molecules were tested by hydrophobic interaction chromatography (HIC) and nSEC-MS, and DARs obtained from both methods were compared to assess the degree to which nSEC-MS quantitation aligned with the HIC release assay. Our results indicated that there is no bias introduced by nSEC-MS quantitation of DAR and that SEC-MS data can be bridged to HIC data without the need for a correction factor or offset. nSEC-MS was also found to be suitable for unbiased DAR quantitation in the other ADC chemotypes that were evaluated. Based on the totality of our work, we conclude that, used as intended, nSEC-MS is well suited for quantitating DAR on a variety of interchain cysteine-linked ADCs in an accurate, unbiased manner.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.