Evidence map›Paper›PMID 30906093›Full record

ArticleJournal of molecular liquids2018

Controlling the viscosities of antibody solutions through control of their binding sites.

Miha Kastelic, Ken A Dill, Yura V Kalyuzhnyi, Vojko Vlachy

Abstract read
In one paragraph

Article in Journal of molecular liquids, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
–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

20 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions.International journal of molecular sciences · 2022
    Pooled it
  2. Fab-Fc and Fab-Fab interactions of variable strength and valency contribute to the high concentration viscosity of IgGProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Electrostatics and viscosity are strongly linked in concentrated antibody solutions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021
    Review
  12. Article
  13. Toward Drug-Like Multispecific Antibodies by Design.International journal of molecular sciences · 2020
    Review
  14. Article
  15. Article
  16. 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
  17. Article
  18. Article
  19. Article
  20. Review
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

4 authors.

Miha KastelicFaculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia.
Ken A DillLaufer Center for Physical and Quantitative Biology and Departments of Physics and Chemistry, Stony Brook University, Stony Brook, NY 11794.
Yura V KalyuzhnyiInstitute for Condensed Matter Physics, Svientsitskii 1, 79011 Lviv, Ukraine.
Vojko VlachyFaculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia.

Funding

Modeling Aqueous Solvation in BiologyR01GM063592 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DILL, KEN A · 2001 to 2018
$4.3M
Modeling Aqueous Solvation in BiologyR56GM063592 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DILL, KEN A · 2009 to 2009
$330k
NIGMS NIH HHS R01 GM063592NIGMS NIH HHS R56 GM063592
6 · The paper itself

Abstract

For biotechnological drugs, it is desirable to formulate antibody solutions with low viscosities. We go beyond previous colloid theories in treating protein-protein self-association of molecules that are antibody-shaped and flexible and have spatially specific binding sites. We consider interactions either through fragment antigen (Fab-Fab) or fragment crystalizable (Fab-Fc) binding. Wertheim's theory is adapted to compute the cluster-size distributions, viscosities, second virial coefficients, and Huggins coefficients, as functions of antibody concentration. We find that the aggregation properties of concentrated solutions can be anticipated from simpler-to-measure dilute solutions. A principal finding is that aggregation is controllable, in principle, through modifying the antibody itself, and not just the solution it is dissolved in. In particular: (i) monospecific antibodies having two identical Fab arms can form linear chains with intermediate viscosities. (ii) Bispecific antibodies having different Fab arms can, in some cases, only dimerize, having low viscosities. (iii) Arm-to-Fc binding allows for three binding partners, leading to networks and high viscosities.

Indexed as

aggregationantibodiessolution viscosityWertheim's theory

Identifiers

PMID30906093
PMCPMC6425977

What OpenQuestion holds

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Registered trials

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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.