Evidence map›Paper›PMID 26552422›Full record

ArticleCellular and molecular life sciences : CMLS2016

Novel affinity binders for neutralization of vascular endothelial growth factor (VEGF) signaling.

Filippa Fleetwood, Rezan Güler, Emma Gordon, Stefan Ståhl, Lena Claesson-Welsh, John Löfblom

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Review
  3. Bacterial Cell Display for Selection of Affibody Molecules.Methods in molecular biology (Clifton, N.J.) · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Affibody molecules as engineered protein drugs.Experimental & molecular medicine · 2017
    Review
  12. 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 3 institutions in 1 country.

Filippa FleetwoodDivision of Protein Technology, School of Biotechnology, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91, Stockholm, Sweden.
Rezan GülerDivision of Protein Technology, School of Biotechnology, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91, Stockholm, Sweden.
Emma GordonDepartment of Immunology, Genetics and Pathology, Rudbeck Laboratory, Uppsala University, Dag Hammarskjöldsv. 20, Uppsala, Sweden.
Stefan StåhlDivision of Protein Technology, School of Biotechnology, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91, Stockholm, Sweden.
Lena Claesson-WelshDepartment of Immunology, Genetics and Pathology, Rudbeck Laboratory, Uppsala University, Dag Hammarskjöldsv. 20, Uppsala, Sweden.
John LöfblomDivision of Protein Technology, School of Biotechnology, KTH, Royal Institute of Technology, AlbaNova University Center, 106 91, Stockholm, Sweden. lofblom@kth.se.
AlbaNova · SEUppsala University · SEKTH Royal Institute of Technology · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiogenesis denotes the formation of new blood vessels from pre-existing vasculature. Progression of diseases such as cancer and several ophthalmological disorders may be promoted by excess angiogenesis. Novel therapeutics to inhibit angiogenesis and diagnostic tools for monitoring angiogenesis during therapy, hold great potential for improving treatment of such diseases. We have previously generated so-called biparatopic Affibody constructs with high affinity for the vascular endothelial growth factor receptor-2 (VEGFR2), which recognize two non-overlapping epitopes in the ligand-binding site on the receptor. Affibody molecules have previously been demonstrated suitable for imaging purposes. Their small size also makes them attractive for applications where an alternative route of administration is beneficial, such as topical delivery using eye drops. In this study, we show that decreasing linker length between the two Affibody domains resulted in even slower dissociation from the receptor. The new variants of the biparatopic Affibody bound to VEGFR2-expressing cells, blocked VEGFA binding, and inhibited VEGFA-induced signaling of VEGFR2 over expressing cells. Moreover, the biparatopic Affibody inhibited sprout formation of endothelial cells in an in vitro angiogenesis assay with similar potency as the bivalent monoclonal antibody ramucirumab. This study demonstrates that the biparatopic Affibody constructs show promise for future therapeutic as well as in vivo imaging applications.

Indexed as

Angiogenesis InhibitorsAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedAntibody AffinityBinding SitesCell LineCell ProliferationExtracellular Signal-Regulated MAP KinasesFlow CytometryHEK293 CellsHumansHuman Umbilical Vein Endothelial CellsNeoplasmsNeovascularization, PathologicPhosphorylationProtein BindingAngiogenesis InhibitorsAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedExtracellular Signal-Regulated MAP KinasesKDR protein, humanRamucirumabRecombinant Fusion ProteinsVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2VEGFA protein, humanAffibody moleculesAngiogenesisBiparatopic affinity proteinBispecificVEGFVEGFR2

Identifiers

PMID26552422
PMCPMC11108507
OpenAlexW2159523710

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.