Evidence map›Paper›PMID 40135773›Full record

ArticleJournal of the American Chemical Society2025

Adding a Twist to Lateral Flow Immunoassays: A Direct Replacement of Antibodies with Helical Affibodies, from Selection to Application.

Christy J Sadler, Adam Creamer, Kim Anh Giang, Kevion K Darmawan, André Shamsabadi, Daniel A Richards, Johan Nilvebrant, Jonathan P Wojciechowski, Patrick Charchar, Ross Burdis and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
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  4. Review
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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

14 authors.

Christy J SadlerDepartment of Materials, Department of Bioengineering, Institute of Biomedical Engineering Imperial College London, London SW7 2AZ, U.K.ORCID 0009-0006-2763-7097
Adam CreamerDepartment of Materials, Department of Bioengineering, Institute of Biomedical Engineering Imperial College London, London SW7 2AZ, U.K.
Kim Anh GiangDepartment of Protein Science, AlbaNova University Center, KTH Royal Institute of Technology, Stockholm SE-114 21, Sweden.ORCID 0000-0002-7097-9408
Kevion K DarmawanSchool of Engineering, RMIT University, Melbourne, VIC 3001, Australia.ORCID 0000-0001-7441-7368
André ShamsabadiDepartment of Materials, Department of Bioengineering, Institute of Biomedical Engineering Imperial College London, London SW7 2AZ, U.K.
Daniel A RichardsDepartment of Materials, Department of Bioengineering, Institute of Biomedical Engineering Imperial College London, London SW7 2AZ, U.K.ORCID 0000-0001-8827-9170
Johan NilvebrantDepartment of Protein Science, AlbaNova University Center, KTH Royal Institute of Technology, Stockholm SE-114 21, Sweden.
Jonathan P WojciechowskiDepartment of Materials, Department of Bioengineering, Institute of Biomedical Engineering Imperial College London, London SW7 2AZ, U.K.ORCID 0000-0002-6272-515X
Patrick CharcharSchool of Engineering, RMIT University, Melbourne, VIC 3001, Australia.ORCID 0000-0002-9201-4711
Ross BurdisDepartment of Materials, Department of Bioengineering, Institute of Biomedical Engineering Imperial College London, London SW7 2AZ, U.K.
Francesca SmithDepartment of Materials, Department of Bioengineering, Institute of Biomedical Engineering Imperial College London, London SW7 2AZ, U.K.
Irene YarovskySchool of Engineering, RMIT University, Melbourne, VIC 3001, Australia.ORCID 0000-0002-4033-5150
Per-Åke NygrenDepartment of Protein Science, AlbaNova University Center, KTH Royal Institute of Technology, Stockholm SE-114 21, Sweden.
Molly M StevensDepartment of Materials, Department of Bioengineering, Institute of Biomedical Engineering Imperial College London, London SW7 2AZ, U.K.ORCID 0000-0002-7335-266X

Funding

Wellcome Trust
6 · The paper itself

Abstract

Immunoreagents, most commonly antibodies, are integral components of lateral flow immunoassays. However, the use of antibodies comes with limitations, particularly relating to their reproducible production, and poor thermal and chemical stability. Here, we employ phage display to develop affibodies, a class of nonimmunoglobulin affinity proteins based on a small three-helix bundle scaffold, against SARS-CoV-2 Spike protein. Subsequently, we demonstrate the utility and viability of affibodies to directly replace antibodies in lateral flow immunoassays. In addition, we highlight several physiochemical advantages of affibodies, including their ability to withstand exposure to high temperature and humidity while maintaining superior performance compared to their antibody counterparts. Furthermore, we investigate the adsorption mechanism of affibodies to the surface of gold nanoparticle probes via a His

Indexed as

AntibodiesRecombinant Fusion ProteinsSARS-CoV-2Spike Glycoprotein, CoronavirusCOVID-19GoldHumansImmunoassayMetal NanoparticlesMolecular Dynamics SimulationAntibodiesGoldRecombinant Fusion ProteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID40135773
PMCPMC11987028

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.