Evidence map›Paper›PMID 34122979›Full record

ArticleChemical science2020

Precipitation-free high-affinity multivalent binding by inline lectin ligands.

Philipp Rohse, Sabrina Weickert, Malte Drescher, Valentin Wittmann

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

5 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Photoswitching Affinity and Mechanism of Multivalent Lectin Ligands.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  5. 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

4 authors at 1 institution in 1 country.

Philipp RohseUniversity of Konstanz, Department of Chemistry, Konstanz Research School Chemical Biology (KoRS-CB) Universitätsstraße 10 78457 Konstanz Germany mail@valentin-wittmann.de.
Sabrina WeickertUniversity of Konstanz, Department of Chemistry, Konstanz Research School Chemical Biology (KoRS-CB) Universitätsstraße 10 78457 Konstanz Germany mail@valentin-wittmann.de.
Malte DrescherUniversity of Konstanz, Department of Chemistry, Konstanz Research School Chemical Biology (KoRS-CB) Universitätsstraße 10 78457 Konstanz Germany mail@valentin-wittmann.de.ORCID https://orcid.org/0000-0002-3571-3452
Valentin WittmannUniversity of Konstanz, Department of Chemistry, Konstanz Research School Chemical Biology (KoRS-CB) Universitätsstraße 10 78457 Konstanz Germany mail@valentin-wittmann.de.ORCID https://orcid.org/0000-0003-4043-6813
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multivalent ligand-protein interactions are a key concept in biology mediating, for example, signalling and adhesion. Multivalent ligands often have tremendously increased binding affinities. However, they also can cause crosslinking of receptor molecules leading to precipitation of ligand-receptor complexes. Plaque formation due to precipitation is a known characteristic of numerous fatal diseases limiting a potential medical application of multivalent ligands with a precipitating binding mode. Here, we present a new design of high-potency multivalent ligands featuring an inline arrangement of ligand epitopes with exceptionally high binding affinities in the low nanomolar range. At the same time, we show with a multi-methodological approach that precipitation of the receptor is prevented. We distinguish distinct binding modes of the ligands, in particular we elucidate a unique chelating binding mode, where four receptor binding sites are simultaneously bridged by one multivalent ligand molecule. The new design concept of inline multivalent ligands, which we established for the well-investigated model lectin wheat germ agglutinin, has great potential for the development of high-potency multivalent inhibitors as future therapeutics.

Identifiers

PMID34122979
PMCPMC8159369
OpenAlexW3017757610

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Registered trials

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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.