ArticleAnalytical and bioanalytical chemistry2018
Affinity profiling of monoclonal antibody and antibody-drug-conjugate preparations by coupled liquid chromatography-surface plasmon resonance biosensing.
Article in Analytical and bioanalytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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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.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Surface plasmon resonance microscopy reveals N-glycosylation driven modulation of affinity and avidity of ErbB receptors in whole single pancreatic cancer cells.Glycobiology · 2025Article
- Structure and function of therapeutic antibodies approved by the US FDA in 2024.Antibody therapeutics · 2025Review
- Single-molecule digital sizing of proteins in solution.Nature communications · 2024Article
- Antibody and antibody fragments site-specific conjugation using new Q-tag substrate of bacterial transglutaminase.Cell death discovery · 2024Article
- Elucidating Novel Targets for Ovarian Cancer Antibody-Drug Conjugate Development: Integrating In Silico Prediction and Surface Plasmon Resonance to Identify Targets with Enhanced Antibody Internalization Capacity.Antibodies (Basel, Switzerland) · 2023Article
- Antibody binding reports spatial heterogeneities in cell membrane organization.Nature communications · 2023Article
- Modeling study of long-term stability of the monoclonal antibody infliximab and biosimilars using liquid-chromatography-tandem mass spectrometry and size-exclusion chromatography-multi-angle light scattering.Analytical and bioanalytical chemistry · 2023Article
- Studying protein structure and function by native separation-mass spectrometry.Nature reviews. Chemistry · 2022Review
- Identification and Affinity Determination of Protein-Antibody and Protein-Aptamer Epitopes by Biosensor-Mass Spectrometry Combination.International journal of molecular sciences · 2021Review
- Glycan Profile Analysis of Engineered Trastuzumab with Rationally Added Glycosylation Sequons Presents Significantly Increased Glycan Complexity.Pharmaceutics · 2021Article
- First-in-Human, Phase 1 Dose-Escalation Study of Biparatopic Anti-HER2 Antibody-Drug Conjugate MEDI4276 in Patients with HER2-positive Advanced Breast or Gastric Cancer.Molecular cancer therapeutics · 2021Article
- Natural and Designed Toxins for Precise Therapy: Modern Approaches in Experimental Oncology.International journal of molecular sciences · 2021Review
- Asymmetric flow field-flow fractionation coupled to surface plasmon resonance detection for analysis of therapeutic proteins in blood serum.Analytical and bioanalytical chemistry · 2021Article
- ATR-FTIR spectroscopy and spectroscopic imaging for the analysis of biopharmaceuticals.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2020Review
- Probing Protein Denaturation during Size-Exclusion Chromatography Using Native Mass Spectrometry.Analytical chemistry · 2020Article
- Effect of gefitinib on serum EGFR and CYFRA21-1 in patients with advanced non-small cell lung cancer.Oncology letters · 2019Article
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Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies (mAbs) and antibody-drug conjugates (ADCs) are highly potent biopharmaceuticals designed for targeted cancer therapies. mAbs and ADCs can undergo modifications during production and storage which may affect binding to target receptors, potentially altering drug efficacy. In this work, liquid chromatography was coupled online to surface plasmon resonance (LC-SPR) to allow label-free affinity evaluation of mAb and ADC sample constituents (size and charge variants), under near-native conditions. Trastuzumab and its ADC trastuzumab emtansine (T-DM1) were used as a test sample and were analyzed by aqueous size-exclusion chromatography (SEC)-SPR before and after exposure to aggregate-inducing conditions. SEC-SPR allowed separation of the formed aggregates and measurement of their affinity towards the ligand-binding domain of the human epidermal growth factor receptor 2 (HER2) receptor immobilized on the surface of the SPR sensor chip. The monomer and aggregates of the mAb and ADC were shown to have similar antigen affinity. Conjugation of drugs to trastuzumab appeared to accelerate the aggregate formation. In addition, cation-exchange chromatography (CEX) was coupled to SPR enabling monitoring the maximum ligand-analyte binding capacity (R
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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.