Evidence map›Paper›PMID 35203649›Full record

ArticleBiomedicines2022

Phage Display-Derived Compounds Displace hACE2 from Its Complex with SARS-CoV-2 Spike Protein.

Marc Sevenich, Elena Thul, Nils-Alexander Lakomek, Thomas Klünemann, Maren Schubert, Federico Bertoglio, Joop van den Heuvel, Patrick Petzsch, Jeannine Mohrlüder, Dieter Willbold

Open access · goldAbstract read
In one paragraph

Article in Biomedicines, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

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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

10 authors at 5 institutions in 1 country.

Marc SevenichInstitute of Biological Information Processing (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0002-7036-6927
Elena ThulMedizinische Fakultät, Westfälische Wilhelms Universität Münster, 48149 Münster, Germany.
Nils-Alexander LakomekInstitute of Biological Information Processing (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Thomas KlünemannHelmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
Maren SchubertInstitut für Biochemie, Biotechnologie und Bioinformatik-Abteilung Biotechnologie, Technische Universität Braunschweig, 38106 Braunschweig, Germany.ORCID 0000-0002-7041-9056
Federico BertoglioInstitut für Biochemie, Biotechnologie und Bioinformatik-Abteilung Biotechnologie, Technische Universität Braunschweig, 38106 Braunschweig, Germany.ORCID 0000-0001-6477-1785
Joop van den HeuvelHelmholtz Centre for Infection Research, 38124 Braunschweig, Germany.ORCID 0000-0001-5085-4010
Patrick PetzschBiologisch-Medizinisches Forschungszentrum (BMFZ), Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0002-8355-5524
Jeannine MohrlüderInstitute of Biological Information Processing (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
Dieter WillboldInstitute of Biological Information Processing (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0002-0065-7366
Forschungszentrum Jülich · DEHelmholtz Centre for Infection Research · DETechnische Universität Braunschweig · DEHeinrich Heine University Düsseldorf · DEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Severe respiratory syndrome coronavirus-2 (SARS-CoV-2) is a highly contagious beta-class coronavirus. Although vaccinations have shown high efficacy, the emergence of novel variants of concern (VOCs) has already exhibited traits of immune evasion. Thus, the development of tailored antiviral medications for patients with incomplete, inefficient, or non-existent immunization, is essential. The attachment of viral surface proteins to the cell surface is the first crucial step in the viral replication cycle, which for SARS-CoV-2 is mediated by the high affinity interaction of the viral trimeric spike with the host cell surface-located human angiotensin converting enzyme-2 (hACE2). Here, we used a novel and efficient next generation sequencing (NGS) supported phage display strategy for the selection of a set of SARS-CoV-2 receptor binding domain (RBD)-targeting peptide ligands that bind to the target protein with low µM to nM dissociation constants. Compound CVRBDL-3 inhibits the SARS-CoV-2 spike protein association to hACE2 in a concentration-dependent manner for pre- as well as post-complex formation conditions. Further rational optimization yielded a CVRBDL-3 based divalent compound, which demonstrated inhibitory efficacy with an IC

Indexed as

acute COVID-19 treatmentcoronavirusphage displaySARS-CoV-2spike-hACE2 inhibitorspike protein

Identifiers

PMID35203649
PMCPMC8962251
OpenAlexW4213248111

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.