Evidence map›Paper›PMID 38194618›Full record

ArticleMolecular pharmaceutics2024

Mechanistic Insights into the Adsorption of Monoclonal Antibodies at the Water/Vapor Interface.

Suman Saurabh, Qinkun Zhang, Zongyi Li, John M Seddon, Cavan Kalonia, Jian R Lu, Fernando Bresme

Open access · hybridAbstract read
In one paragraph

Article in Molecular pharmaceutics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. 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

7 authors at 3 institutions in 2 countries.

Suman SaurabhDepartment of Chemistry, Molecular Sciences Research Hub Imperial College, London W12 0BZ, U.K.ORCID 0000-0003-1399-0464
Qinkun ZhangDepartment of Chemistry, Molecular Sciences Research Hub Imperial College, London W12 0BZ, U.K.
Zongyi LiBiological Physics Group, School of Physics and Astronomy, Faculty of Science and Engineering, the University of Manchester, Manchester M13 9PL, U.K.ORCID 0000-0002-5989-9132
John M SeddonDepartment of Chemistry, Molecular Sciences Research Hub Imperial College, London W12 0BZ, U.K.
Cavan KaloniaDosage Form Design and Development, BioPharmaceutical Development, BioPharmaceuticals R&D, AstraZeneca, Gaithersburg, Maryland 20878, United States.
Jian R LuBiological Physics Group, School of Physics and Astronomy, Faculty of Science and Engineering, the University of Manchester, Manchester M13 9PL, U.K.ORCID 0000-0001-5648-3564
Fernando BresmeDepartment of Chemistry, Molecular Sciences Research Hub Imperial College, London W12 0BZ, U.K.ORCID 0000-0001-9496-4887
Imperial College London · GBUniversity of Manchester · GBAstraZeneca (United States) · US

Funding

Biotechnology and Biological Sciences Research Council BB/S018468/1Biotechnology and Biological Sciences Research Council BB/S018492/1
6 · The paper itself

Abstract

Monoclonal antibodies (mAbs) are active components of therapeutic formulations that interact with the water-vapor interface during manufacturing, storage, and administration. Surface adsorption has been demonstrated to mediate antibody aggregation, which leads to a loss of therapeutic efficacy. Controlling mAb adsorption at interfaces requires a deep understanding of the microscopic processes that lead to adsorption and identification of the protein regions that drive mAb surface activity. Here, we report all-atom molecular dynamics (MD) simulations of the adsorption behavior of a full IgG1-type antibody at the water/vapor interface. We demonstrate that small local changes in the protein structure play a crucial role in promoting adsorption. Also, interfacial adsorption triggers structural changes in the antibody, potentially contributing to the further enhancement of surface activity. Moreover, we identify key amino acid sequences that determine the adsorption of antibodies at the water-air interface and outline strategies to control the surface activity of these important therapeutic proteins.

Indexed as

Antibodies, MonoclonalSteamAdsorptionDrug CompoundingWaterAntibodies, MonoclonalSteamWaterhydrophobicitymonoclonal antibodyprotein adsorptionsolvent accessible surface areasurface activitysurface tensionwater/vapor interface

Identifiers

PMID38194618
PMCPMC10848294
OpenAlexW4390706677

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.