Evidence map›Paper›PMID 36580213›Full record

ArticleDoklady. Biochemistry and biophysics2022

Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain.

M V Sidorova, R S Bibilashvili, D V Avdeev, U S Kozhokar, M E Palkeeva, M V Ovchinnikov, A S Molokoedov, D A Shirokov, A V Semyonova, V I Uvarova and 10 more

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In one paragraph

Article in Doklady. Biochemistry and biophysics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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

20 authors at 8 institutions in 1 country.

M V SidorovaChazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia.
R S BibilashviliChazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia.
D V AvdeevChazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia.
U S KozhokarChazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia.
M E PalkeevaChazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia.
M V OvchinnikovChazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia.
A S MolokoedovChazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia.
D A ShirokovFederal Research and Clinical Center of Physical Chemical Medicine, Federal Medical Biological Agency, Moscow, Russia.
A V SemyonovaFederal Research and Clinical Center of Physical Chemical Medicine, Federal Medical Biological Agency, Moscow, Russia.
V I UvarovaChumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia.
P O KulyaevSirius University of Science and Technology, Sochi, Russia.
E V KhvatovChumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia.
A A IgnatovaInstitute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
A V FeofanovLomonosov Moscow State University, Moscow, Russia.
D I OsolodkinChumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia.
Yu B PorozovSirius University of Science and Technology, Sochi, Russia.
L I KozlovskayaChumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia. kozlovskaya_li@chumakovs.su.
A A IshmukhametovChumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia.
Ye V ParfyonovaChazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia.
A M EgorovChumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia.
National Medical Research Center of Cardiology · RURussian Academy of Sciences · RUFederal Medical-Biological Agency · RUInstitute of Bioorganic Chemistry · RULomonosov Moscow State University · RUMoscow State Academy of Veterinary Medicine and Biotechnology named after Skryabin · RUSechenov University · RUSirius University of Science and Technology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aim of this work was to design and characterize peptides based on the α-helices h1 and h2 of the ACE2 receptor, forming the interaction interface between the receptor-binding domain (RBD) of the SARS-CoV-2 S protein and the cellular ACE2 receptor. Monomeric and heterodimeric peptides connected by disulfide bonds at different positions were synthesized. Solubility, RBD-binding affinity, and peptide helicity were experimentally measured, and molecular dynamics simulation was performed in various solvents. It was established that the preservation of the helical conformation is a necessary condition for the binding of peptides to RBD. The peptides have a low degree of helicity and low affinity for RBD in water. Dimeric peptides have a higher degree of helicity than monomeric ones, probably due to the mutual influence of helices. The degree of helicity of the peptides in trifluoroethanol is the highest; however, for in vitro studies, the most suitable solvent is a water-ethanol mixture.

Indexed as

Angiotensin-Converting Enzyme 2COVID-19HumansMolecular Dynamics SimulationPeptidesProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2PeptidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2dissociation constanthelicitypeptide inhibitorsRBDSARS-CoV-2

Identifiers

PMID36580213
PMCPMC9798946
OpenAlexW4313267776

What OpenQuestion holds

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LicenceCC BY
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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.