Evidence map›Paper›PMID 39777463›Full record

ArticleNucleic acids research2025

Unveiling the unusual i-motif-derived architecture of a DNA aptamer exhibiting high affinity for influenza A virus.

Vladimir Tsvetkov, Bartomeu Mir, Rugiya Alieva, Alexander Arutyunyan, Ilya Oleynikov, Roman Novikov, Elizaveta Boravleva, Polina Kamzeeva, Timofei Zatsepin, Andrey Aralov and 2 more

Abstract read
In one paragraph

Article in Nucleic acids research, 2025. 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
–field-weighted citation impact
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.

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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

12 authors.

Vladimir TsvetkovCenter for Mathematical Modeling in Drug Development, Sechenov First Moscow State Medical University, Moscow 119991, Russia.ORCID 0000-0003-0494-3332
Bartomeu MirInstituto de Química Física Blas Cabrera, CSIC, Madrid 28006, Spain.
Rugiya AlievaChemistry Department, Lomonosov Moscow State University, Moscow 119991, Russia.
Alexander ArutyunyanBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia.
Ilya OleynikovBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia.
Roman NovikovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia.
Elizaveta BoravlevaChumakov Federal Scientific Center for Research and Development of Immunobiological Products (Institute of Poliomyelitis), Russian Academy of Sciences, Moscow 108819, Russia.
Polina KamzeevaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.
Timofei ZatsepinChemistry Department, Lomonosov Moscow State University, Moscow 119991, Russia.
Andrey AralovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.ORCID 0000-0003-3268-2352
Carlos GonzálezInstituto de Química Física Blas Cabrera, CSIC, Madrid 28006, Spain.ORCID 0000-0001-8796-1282
Elena ZavyalovaChemistry Department, Lomonosov Moscow State University, Moscow 119991, Russia.ORCID 0000-0001-5260-1973

Funding

Federal State Autonomous Educational Institution of Higher Education I.M 121031300037-7Ministry of Health of the Russian FederationSechenov First Moscow State Medical University
6 · The paper itself

Abstract

Non-canonical nucleic acid structures play significant roles in cellular processes through selective interactions with proteins. While both natural and artificial G-quadruplexes have been extensively studied, the functions of i-motifs remain less understood. This study investigates the artificial aptamer BV42, which binds strongly to influenza A virus hemagglutinin and unexpectedly retains its i-motif structure even at neutral pH. However, BV42 conformational heterogeneity hinders detailed structural analysis. Molecular dynamics simulations and chemical modifications of BV42 helped us to identify a potential binding site, allowing for aptamer redesign to eliminate the conformational diversity while retaining binding affinity. Nuclear magnetic resonance spectroscopy confirmed the i-motif/duplex junction with the three-cytosine loop nearby. This study highlights the unique structural features of the functional i-motif and its role in molecular recognition of the target.

Indexed as

Aptamers, NucleotideInfluenza A virusMolecular Dynamics SimulationBinding SitesG-QuadruplexesHemagglutinin Glycoproteins, Influenza VirusNucleic Acid ConformationNucleotide MotifsAptamers, NucleotideHemagglutinin Glycoproteins, Influenza Virus

Identifiers

PMID39777463
PMCPMC11704962

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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.