ArticleJournal of chromatography. A2015
Protein A chromatography increases monoclonal antibody aggregation rate during subsequent low pH virus inactivation hold.
Article in Journal of chromatography. A, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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
45 citing papers in PubMed, 164 citations in OpenAlex.
- Rapid purity and charge-variant analysis of bispecific antibodies using microfluidic capillary electrophoresis-mass spectrometry.Analytical and bioanalytical chemistry · 2026Article
- Analysing the structure of antibodies using circular dichroism with an antibody augmented reference set and the algorithm SELCON.European biophysics journal : EBJ · 2026Article
- Characterization of Conformational Instability of Monoclonal Antibodies During Chromatographic Purification.International journal of molecular sciences · 2026Review
- Chromatography's evolution, unlocking affinity's new solution: potential-controlled affinity membrane chromatography.RSC advances · 2026Article
- Understanding the Role of Polyols and Sugars in Reducing Aggregation in IgGPharmaceuticals (Basel, Switzerland) · 2025Article
- Impact of Initial Aggregate Level on Aggregation Potential of Monoclonal Antibodies in Different Buffer Systems.Pharmaceutical research · 2025Article
- Comparative Forced Degradation Study of Anticomplement C5 Biosimilar and Originator Monoclonal Antibodies.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Antibody Aggregation: A Problem Within the Biopharmaceutical Industry and Its Role in AL Amyloidosis Disease.The protein journal · 2025Review
- IgG-Binding Peptidomimetic Mixed-Charge Polymer-Modified Resins for Chromatographic Purification of Antibodies.ACS applied materials & interfaces · 2024Article
- Engineering and physicochemical characterization of a novel, stable, symmetric bispecific antibody with dual target-binding using a common light chain.Protein science : a publication of the Protein Society · 2024Article
- Analysis of the Structure of 14 Therapeutic Antibodies Using Circular Dichroism Spectroscopy.Analytical chemistry · 2024Article
- Study of Monoclonal Antibody Aggregation at the Air-Liquid Interface under Flow by ATR-FTIR Spectroscopic Imaging.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Biophysical Analysis of Therapeutic Antibodies in the Early Development Pipeline.Biologics : targets & therapy · 2024Review
- Quantitative Recoveries of Exosomes and Monoclonal Antibodies from Chinese Hamster Ovary Cell Cultures by Use of a Single, Integrated Two-Dimensional Liquid Chromatography Method.Analytical chemistry · 2023Article
- Enhancing thermal stability in the CHProtein science : a publication of the Protein Society · 2023Article
- Neuronal binding by antibodies can be influenced by low pH stress during the isolation procedure.Journal of immunological methods · 2023Article
- Behavior of host-cell-protein-rich aggregates in antibody capture and polishing chromatography.Journal of chromatography. A · 2023Article
- Product safety aspects of plant molecular farming.Frontiers in bioengineering and biotechnology · 2023Review
- Decreasing hydrophobicity or shielding hydrophobic areas of CH2 attenuates low pH-induced IgG4 aggregation.Frontiers in bioengineering and biotechnology · 2023Article
- Nanoplasmonic Avidity-Based Detection and Quantification of IgG Aggregates.Analytical chemistry · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Protein A chromatography is a near-ubiquitous method of mAb capture in bioprocesses. The use of low pH buffer for elution from protein A is known to contribute to product aggregation. Yet, a more limited set of evidence suggests that low pH may not be the sole cause of aggregation in protein A chromatography, rather, other facets of the process may contribute significantly. This paper presents a well-defined method for investigating this problem. An IgG4 was incubated in elution buffer after protein A chromatography (typical of the viral inactivation hold) and the quantity of monomer in neutralised samples was determined by size exclusion chromatography; elution buffers of different pH values predetermined to induce aggregation of the IgG4 were used. Rate constants for monomer decay over time were determined by fitting exponential decay functions to the data. Similar experiments were implemented in the absence of a chromatography step, i.e. IgG4 aggregation at low pH. Rate constants for aggregation after protein A chromatography were considerably higher than those from low pH exposure alone; a distinct shift in aggregation rates was apparent across the pH range tested.
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.