Evidence map›Paper›PMID 23196810›Full record

ArticlemAbs

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces.

Ruairidh G Couston, Maximilian W Skoda, Shahid Uddin, Christopher F van der Walle

Open access · goldAbstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  8. Inhaled antibodies: Quality and performance considerations.Human vaccines & immunotherapeutics · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Fluctuations in Pharmacokinetics Profiles of Monoclonal Antibodies.European journal of drug metabolism and pharmacokinetics · 2019
    Article
  17. Oriented attachment of VChemical communications (Cambridge, England) · 2019
    Article
  18. Article
  19. 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

4 authors at 4 institutions in 1 country.

Ruairidh G CoustonStrathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, Scotland, UK.
Maximilian W Skoda
Shahid Uddin
Christopher F van der Walle
Glasgow Life · GBGranta Design (United Kingdom) · GBResearch Complex at Harwell · GBUniversity of Strathclyde · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One aspiration for the formulation of human monoclonal antibodies (mAb) is to reach high solution concentrations without compromising stability. Protein surface activity leading to instability is well known, but our understanding of mAb adsorption to the solid-liquid interface in relevant pH and surfactant conditions is incomplete. To investigate these conditions, we used total internal reflection fluorescence (TIRF) and neutron reflectometry (NR). The mAb tested ("mAb-1") showed highest surface loading to silica at pH 7.4 (~12 mg/m(2)), with lower surface loading at pH 5.5 (~5.5 mg/m(2), further from its pI of 8.99) and to hydrophobized silica (~2 mg/m(2)). The extent of desorption of mAb-1 from silica or hydrophobized silica was related to the relative affinity of polysorbate 20 or 80 for the same surface. mAb-1 adsorbed to silica on co-injection with polysorbate (above its critical micelle concentration) and also to silica pre-coated with polysorbate. A bilayer model was developed from NR data for mAb-1 at concentrations of 50-5000 mg/L, pH 5.5, and 50-2000 mg/L, pH 7.4. The inner mAb-1 layer was adsorbed to the SiO₂ surface at near saturation with an end-on" orientation, while the outer mAb-1 layer was sparse and molecules had a "side-on" orientation. A non-uniform triple layer was observed at 5000 mg/L, pH 7.4, suggesting mAb-1 adsorbed to the SiO₂ surface as oligomers at this concentration and pH. mAb-1 adsorbed as a sparse monolayer to hydrophobized silica, with a layer thickness increasing with bulk concentration - suggesting a near end-on orientation without observable relaxation-unfolding.

Indexed as

AdsorptionAntibodies, MonoclonalFluorescenceHumansHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsNeutronsPolysorbatesSilicon DioxideSurface-Active AgentsSurface PropertiesAntibodies, MonoclonalPolysorbatesSilicon DioxideSurface-Active Agents

Identifiers

PMID23196810
PMCPMC3564877
OpenAlexW1968611542

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.