Evidence map›Paper›PMID 24089716›Full record

ArticleThe Journal of chemical physics2013

Phase transitions in human IgG solutions.

Ying Wang, Aleksey Lomakin, Ramil F Latypov, Jacob P Laubach, Teru Hideshima, Paul G Richardson, Nikhil C Munshi, Kenneth C Anderson, George B Benedek

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of chemical physics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
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

24 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  3. Review
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  5. Article
  6. Article
  7. Interaction of Positively Charged Oligopeptides with Blood Plasma Proteins.International journal of molecular sciences · 2023
    Article
  8. Article
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  14. A stepwise mechanism for aqueous two-phase system formation in concentrated antibody solutions.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Modeling the depletion effect caused by an addition of polymer to monoclonal antibody solutions.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
  16. Article
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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

9 authors at 4 institutions in 1 country.

Ying WangMaterials Processing Center, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Aleksey Lomakin
Ramil F Latypov
Jacob P Laubach
Teru Hideshima
Paul G Richardson
Nikhil C Munshi
Kenneth C Anderson
George B Benedek
Massachusetts Institute of Technology · USMaterials Processing (United States) · USAmgen (United States) · USDana-Farber Cancer Institute · US

Funding

Targeting Genomic Instability and Evolution in MyelomaP01CA155258 · NCI · DANA-FARBER CANCER INST · PI Jill Corre · 2011 to 2026
$32.5M
NCI NIH HHS P01 CA155258
6 · The paper itself

Abstract

Protein condensations, such as crystallization, liquid-liquid phase separation, aggregation, and gelation, have been observed in concentrated antibody solutions under various solution conditions. While most IgG antibodies are quite soluble, a few outliers can undergo condensation under physiological conditions. Condensation of IgGs can cause serious consequences in some human diseases and in biopharmaceutical formulations. The phase transitions underlying protein condensations in concentrated IgG solutions is also of fundamental interest for the understanding of the phase behavior of non-spherical protein molecules. Due to the high solubility of generic IgGs, the phase behavior of IgG solutions has not yet been well studied. In this work, we present an experimental approach to study IgG solutions in which the phase transitions are hidden below the freezing point of the solution. Using this method, we have investigated liquid-liquid phase separation of six human myeloma IgGs and two recombinant pharmaceutical human IgGs. We have also studied the relation between crystallization and liquid-liquid phase separation of two human cryoglobulin IgGs. Our experimental results reveal several important features of the generic phase behavior of IgG solutions: (1) the shape of the coexistence curve is similar for all IgGs but quite different from that of quasi-spherical proteins; (2) all IgGs have critical points located at roughly the same protein concentration at ~100 mg/ml while their critical temperatures vary significantly; and (3) the liquid-liquid phase separation in IgG solutions is metastable with respect to crystallization. These features of phase behavior of IgG solutions reflect the fact that all IgGs have nearly identical molecular geometry but quite diverse net inter-protein interaction energies. This work provides a foundation for further experimental and theoretical studies of the phase behavior of generic IgGs as well as outliers with large propensity to condense. The investigation of the phase diagram of IgG solutions is of great importance for the understanding of immunoglobulin deposition diseases as well as for the understanding of the colloidal stability of IgG pharmaceutical formulations.

Indexed as

Crystallography, X-RayHumansImmunoglobulin GModels, MolecularMultiple MyelomaPhase TransitionSolutionsTemperatureImmunoglobulin GSolutions

Identifiers

PMID24089716
PMCPMC4108626
OpenAlexW2025100278

What OpenQuestion holds

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Registered trials

None linked

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.