Evidence map›Paper›PMID 31609054›Full record

ArticleAngewandte Chemie (International ed. in English)2019

Site-Specific Encoding of Photoactivity in Antibodies Enables Light-Mediated Antibody-Antigen Binding on Live Cells.

Thomas Bridge, Saher A Shaikh, Paul Thomas, Joaquin Botta, Peter J McCormick, Amit Sachdeva

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Engineering Homogeneous Photoactive Antibody Fragments.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Article
  14. A Light-Activatable Photocaged Variant of the Ultra-High Affinity ALFA-Tag Nanobody.Chembiochem : a European journal of chemical biology · 2022
    Article
  15. Cystine Knot Peptides with Tuneable Activity and Mechanism.Angewandte Chemie (International ed. in English) · 2022
    Article
  16. Article
  17. Structure-based design of a photoswitchable affibody scaffold.Protein science : a publication of the Protein Society · 2021
    Article
  18. Review
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Thomas BridgeSchool of Chemistry, University of East Anglia, Norwich, NR4 7TJ, UK.
Saher A ShaikhSchool of Chemistry, University of East Anglia, Norwich, NR4 7TJ, UK.
Paul ThomasThe Henry Wellcome Laboratory of Cell Imaging, University of East Anglia, Norwich, NR4 7TJ, UK.
Joaquin BottaCentre of Endocrinology, William Harvey Research Institute, Queen Mary University London, Charterhouse Square, London, EC1M 6BQ, UK.
Peter J McCormickCentre of Endocrinology, William Harvey Research Institute, Queen Mary University London, Charterhouse Square, London, EC1M 6BQ, UK.
Amit SachdevaSchool of Chemistry, University of East Anglia, Norwich, NR4 7TJ, UK.ORCID 0000-0002-7575-2819
University of East Anglia · GBWilliam Harvey Research Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R004692/1Wellcome Trust 204593/Z/16/Z
6 · The paper itself

Abstract

Antibodies have found applications in several fields, including, medicine, diagnostics, and nanotechnology, yet methods to modulate antibody-antigen binding using an external agent remain limited. Here, we have developed photoactive antibody fragments by genetic site-specific replacement of single tyrosine residues with photocaged tyrosine, in an antibody fragment, 7D12. A simple and robust assay is adopted to evaluate the light-mediated binding of 7D12 mutants to its target, epidermal growth factor receptor (EGFR), on the surface of cancer cells. Presence of photocaged tyrosine reduces 7D12-EGFR binding affinity by over 20-fold in two out of three 7D12 mutants studied, and binding is restored upon exposure to 365 nm light. Molecular dynamics simulations explain the difference in effect of photocaging on 7D12-EGFR interaction among the mutants. Finally, we demonstrate the application of photoactive antibodies in delivering fluorophores to EGFR-positive live cancer cells in a light-dependent manner.

Indexed as

Antibodies, MonoclonalAntigensCell Line, TumorErbB ReceptorsHumansLightMicroscopy, FluorescenceMolecular Dynamics SimulationMutationTyrosineAntibodies, MonoclonalAntigensEGFR protein, humanErbB ReceptorsTyrosineantibodiescancerprotein designsynthetic biologyunnatural amino acids

Identifiers

PMID31609054
PMCPMC6973043
OpenAlexW2979895193

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.