Evidence map›Paper›PMID 23054090›Full record

ArticlePharmaceutical research2013

Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: from oligomers to larger aggregates.

Paolo Arosio, Simonetta Rima, Massimo Morbidelli

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Article in Pharmaceutical research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Antibody Aggregate Removal by Multimodal Chromatography.Molecules (Basel, Switzerland) · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Characterizing Thermal Transitions of IgG with Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Paolo ArosioDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, ETH Zurich, 8093, Zurich, Switzerland.
Simonetta Rima
Massimo Morbidelli

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeTo identify the aggregation mechanism and the stability characteristics of three different monoclonal antibodies under acidic conditions.

methodsThe aggregation kinetics is analyzed by a combination of light scattering, size exclusion chromatography and fluorescence techniques and the aggregation data are correlated to protein structure, hydrophobicity, charge and antibody subclass.

resultsIn the investigated conditions, the antibody aggregation follows a mechanism consisting of two-steps: reversible monomer oligomerization followed by irreversible cluster-cluster aggregation. The kinetics of the two steps is differently affected by the operating conditions: mild destabilizing conditions induce formation of oligomers which are stable within weeks, while stronger denaturing conditions promote aggregation of oligomers to larger aggregates which eventually precipitate. For different antibodies significant differences in both oligomerization and growth rates are found, even for antibodies belonging to the same subclass. For all antibodies the aggregate formation is accompanied by a structure re-organization with an increase in the ordered β-sheet structures. At low pH the aggregation propensity of the investigated antibodies does not correlate with antibody subclass, surface net charge and hydrophobicity of the non-native state.

conclusionsThe aggregation mechanism of three antibodies in acidic conditions as well as differences and analogies in their stability behavior has been characterized.

Indexed as

Antibodies, MonoclonalChromatography, GelHydrogen-Ion ConcentrationImmunoglobulin GKineticsProtein DenaturationProtein StabilityProtein Structure, SecondaryAntibodies, MonoclonalImmunoglobulin G

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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.