Evidence map›Paper›PMID 32749019›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Rational Design of a DNA-Scaffolded High-Affinity Binder for Langerin.

Gunnar Bachem, Eike-Christian Wamhoff, Kim Silberreis, Dongyoon Kim, Hannes Baukmann, Felix Fuchsberger, Jens Dernedde, Christoph Rademacher, Oliver Seitz

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Bispecific DNA-Peptide Probes for Targeting Receptor Pairs on Live Cells.Angewandte Chemie (International ed. in English) · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Rational Design of a DNA-Scaffolded High-Affinity Binder for Langerin.Angewandte Chemie (International ed. in English) · 2020
    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

9 authors at 2 institutions in 1 country.

Gunnar BachemDepartment of Chemistry, Humboldt-Universität zu Berlin, 12489, Berlin, Germany.
Eike-Christian WamhoffDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany.
Kim SilberreisInstitute of Laboratory Medicine, Clinical Chemistry and Pathobiochemistry, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 13353, Berlin, Germany.
Dongyoon KimDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany.
Hannes BaukmannDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany.
Felix FuchsbergerDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany.
Jens DerneddeInstitute of Laboratory Medicine, Clinical Chemistry and Pathobiochemistry, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 13353, Berlin, Germany.
Christoph RademacherDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany.
Oliver SeitzDepartment of Chemistry, Humboldt-Universität zu Berlin, 12489, Berlin, Germany.ORCID 0000-0003-0611-4810
Max Planck Society · DEHumboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Binders of langerin could target vaccines to Langerhans cells for improved therapeutic effect. Since langerin has low affinity for monovalent glycan ligands, highly multivalent presentation has previously been key for targeting. Aiming to reduce the amount of ligand required, we rationally designed molecularly defined high-affinity binders based on the precise display of glycomimetic ligands (Glc2NTs) on DNA-PNA scaffolds. Rather than mimicking langerin's homotrimeric structure with a C3-symmetric scaffold, we developed readily accessible, easy-to-design bivalent binders. The method considers the requirements for bridging sugar binding sites and statistical rebinding as a means to both strengthen the interactions at single binding sites and amplify the avidity enhancement provided by chelation. This gave a 1150-fold net improvement over the affinity of the free ligand and provided a nanomolar binder (IC

Indexed as

Antigens, CDBinding SitesDNAHumansLangerhans CellsLectins, C-TypeLigandsMannose-Binding LectinsModels, MolecularMolecular ConformationAntigens, CDCD207 protein, humanDNALectins, C-TypeLigandsMannose-Binding Lectinscarbohydrate recognitionDNA nanotechnologylectinsmultivalent interactionspeptide nucleic acids

Identifiers

PMID32749019
PMCPMC7693190
OpenAlexW3047288532

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.