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Helquat dyes targeting G-quadruplexes as a new class of anti-HIV-1 inhibitors

  1. 1.
    SYSNO ASEP0571224
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleHelquat dyes targeting G-quadruplexes as a new class of anti-HIV-1 inhibitors
    Author(s) Pávová, Marcela (UOCHB-X)
    Reyes Gutierrez, Paul Eduardo (UOCHB-X) RID, ORCID
    Kozák, Jaroslav (UOCHB-X) RID, ORCID
    Dobiaš, Juraj (UOCHB-X) ORCID
    Yurenko, Yevgen (UOCHB-X)
    Lepšík, Martin (UOCHB-X) RID, ORCID
    Teplý, Filip (UOCHB-X) RID, ORCID
    Weber, Jan (UOCHB-X) RID, ORCID
    Article number6096
    Source TitleScientific Reports. - : Nature Publishing Group - ISSN 2045-2322
    Roč. 13, April (2023)
    Number of pages13 s.
    Languageeng - English
    CountryUS - United States
    Keywordslong terminal repeat ; promoter ; binding
    OECD categoryVirology
    R&D ProjectsLX22NPO5103 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Research Infrastructuree-INFRA CZ - 90140 - CESNET, zájmové sdružení právnických osob
    Method of publishingOpen access
    Institutional supportUOCHB-X - RVO:61388963
    UT WOS000984454500085
    EID SCOPUS85152381657
    DOI10.1038/s41598-023-33263-3
    AnnotationThe secondary structure of nucleic acids containing quartets of guanines, termed G-quadruplexes, is known to regulate the transcription of many genes. Several G-quadruplexes can be formed in the HIV-1 long terminal repeat promoter region and their stabilization results in the inhibition of HIV-1 replication. Here, we identified helquat-based compounds as a new class of anti-HIV-1 inhibitors that inhibit HIV-1 replication at the stage of reverse transcription and provirus expression. Using Taq polymerase stop and FRET melting assays, we have demonstrated their ability to stabilize G-quadruplexes in the HIV-1 long-terminal repeat sequence. Moreover, these compounds were not binding to the general G-rich region, but rather to G-quadruplex-forming regions. Finally, docking and molecular dynamics calculations indicate that the structure of the helquat core greatly affects the binding mode to the individual G-quadruplexes. Our findings can provide useful information for the further rational design of inhibitors targeting G-quadruplexes in HIV-1.
    WorkplaceInstitute of Organic Chemistry and Biochemistry
    Contactasep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418
    Year of Publishing2024
    Electronic addresshttps://doi.org/10.1038/s41598-023-33263-3
Number of the records: 1  

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