Evidence map›Paper›PMID 34452912›Full record

ArticleScience advances2021

No ordinary proteins: Adsorption and molecular orientation of monoclonal antibodies.

Ankit Kanthe, Andrew Ilott, Mary Krause, Songyan Zheng, Jinjiang Li, Wei Bu, Mrinal K Bera, Binhua Lin, Charles Maldarelli, Raymond S Tu

Abstract read
In one paragraph

Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Antibodies Adsorbed to the Air-Water Interface Form Soft Glasses.Langmuir : the ACS journal of surfaces and colloids · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

10 authors.

Ankit KantheDepartment of Chemical Engineering, The City College of New York, New York, NY 10031, USA.ORCID https://orcid.org/0000-0003-4451-5383
Andrew IlottDrug Product Development, Bristol Myers Squibb, New Brunswick, NJ 08901, USA.
Mary KrauseDrug Product Development, Bristol Myers Squibb, New Brunswick, NJ 08901, USA.ORCID https://orcid.org/0000-0002-3299-5423
Songyan ZhengDrug Product Development, Bristol Myers Squibb, New Brunswick, NJ 08901, USA.
Jinjiang LiPharmaceutical Development, Wolfe Laboratories, Watertown, MA, 01801, USA.ORCID https://orcid.org/0000-0002-8079-9144
Wei BuNSF's ChemMatCARS, Center for Advanced Radiation Sources, University of Chicago, Chicago, IL 606371, USA.ORCID https://orcid.org/0000-0002-9996-3733
Mrinal K BeraNSF's ChemMatCARS, Center for Advanced Radiation Sources, University of Chicago, Chicago, IL 606371, USA.ORCID https://orcid.org/0000-0003-0698-5253
Binhua LinNSF's ChemMatCARS, Center for Advanced Radiation Sources, University of Chicago, Chicago, IL 606371, USA.ORCID https://orcid.org/0000-0001-5932-4905
Charles MaldarelliDepartment of Chemical Engineering, The City College of New York, New York, NY 10031, USA. cmaldarelli@ccny.cuny.edu tu@ccny.cuny.edu.ORCID https://orcid.org/0000-0001-7427-2349
Raymond S TuDepartment of Chemical Engineering, The City College of New York, New York, NY 10031, USA. cmaldarelli@ccny.cuny.edu tu@ccny.cuny.edu.ORCID https://orcid.org/0000-0002-6192-7665

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction of monoclonal antibodies (mAbs) with air/water interfaces plays a crucial role in their overall stability in solution. We aim to understand this behavior using pendant bubble measurements to track the dynamic tension reduction and x-ray reflectivity to obtain the electron density profiles (EDPs) at the surface. Native immunoglobulin G mAb is a rigid molecule with a flat, "Y" shape, and simulated EDPs are obtained by rotating a homology construct at the surface. Comparing simulations with experimental EDPs, we obtain surface orientation probability maps showing mAbs transition from flat-on Y-shape configurations to side-on or end-on configurations with increasing concentration. The modeling also shows the presence of β sheets at the surface. Overall, the experiments and the homology modeling elucidate the orientational phase space during different stages of adsorption of mAbs at the air/water interface. These finding will help define new strategies for the manufacture and storage of antibody-based therapeutics.

Identifiers

PMID34452912
PMCPMC8397265

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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.