Evidence map›Paper›PMID 36288301›Full record

ArticleScience advances2022

De novo selected hACE2 mimics that integrate hotspot peptides with aptameric scaffolds for binding tolerance of SARS-CoV-2 variants.

Minjong Lee, Byunghwa Kang, Juhwa Lee, Jisun Lee, Sang Taek Jung, Chang Yun Son, Seung Soo Oh

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

8 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  3. Review
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  6. Review
  7. Article
  8. Enzymatic Synthesis of Vancomycin-Modified DNA.Molecules (Basel, Switzerland) · 2022
    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

7 authors at 2 institutions in 2 countries.

Minjong LeeDepartment of Materials Science and Engineering, Pohang University of Science and Technology (POSTECH), Pohang 37673, South Korea.ORCID 0000-0002-1729-9876
Byunghwa KangDepartment of Materials Science and Engineering, Pohang University of Science and Technology (POSTECH), Pohang 37673, South Korea.
Juhwa LeeDepartment of Chemistry, Pohang University of Science and Technology (POSTECH), Pohang 37673, South Korea.ORCID 0000-0002-0982-743X
Jisun LeeDepartment of Biomedical Sciences, Graduate School, Korea University, Seoul 02841, South Korea.
Sang Taek JungDepartment of Biomedical Sciences, Graduate School, Korea University, Seoul 02841, South Korea.ORCID 0000-0001-7217-979X
Chang Yun SonDepartment of Chemistry, Pohang University of Science and Technology (POSTECH), Pohang 37673, South Korea.ORCID 0000-0002-0784-6565
Seung Soo OhDepartment of Materials Science and Engineering, Pohang University of Science and Technology (POSTECH), Pohang 37673, South Korea.ORCID 0000-0001-8045-080X
Pohang University of Science and Technology · KRKorea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The frequent occurrence of viral variants is a critical problem in developing antiviral prophylaxis and therapy; along with stronger recognition of host cell receptors, the variants evade the immune system-based vaccines and neutralizing agents more easily. In this work, we focus on enhanced receptor binding of viral variants and demonstrate generation of receptor-mimicking synthetic reagents, capable of strongly interacting with viruses and their variants. The hotspot interaction of viruses with receptor-derived short peptides is maximized by aptamer-like scaffolds, the compact and stable architectures of which can be in vitro selected from a myriad of the hotspot peptide-coupled random nucleic acids. We successfully created the human angiotensin-converting enzyme 2 (hACE2) receptor-mimicking hybrid ligand that recruits the hACE2-derived receptor binding domain-interacting peptide to directly interact with a binding hotspot of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Experiencing affinity boosting by ~500% to Omicron, the de novo selected hACE2 mimic exhibited a great binding tolerance to all SARS-CoV-2 variants of concern.

Indexed as

COVID-19Nucleic AcidsAngiotensin-Converting Enzyme 2Antiviral AgentsHumansLigandsPeptidesPeptidyl-Dipeptidase AProtein BindingReceptors, VirusSARS-CoV-2Spike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2Antiviral AgentsLigandsNucleic AcidsPeptidesPeptidyl-Dipeptidase AReceptors, VirusSpike Glycoprotein, Coronavirus

Identifiers

PMID36288301
PMCPMC9604513
OpenAlexW4307309210

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.