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Ligand Strain and Its Conformational Complexity Is a Major Factor in the Binding of Cyclic Dinucleotides to STING Protein

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    SYSNO ASEP0541558
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleLigand Strain and Its Conformational Complexity Is a Major Factor in the Binding of Cyclic Dinucleotides to STING Protein
    Author(s) Smola, Miroslav (UOCHB-X) ORCID
    Gutten, Ondrej (UOCHB-X) RID, ORCID
    Dejmek, Milan (UOCHB-X) RID, ORCID
    Kožíšek, Milan (UOCHB-X) RID, ORCID
    Evangelidis, Thomas (UOCHB-X) ORCID
    Tehrani, Zahra Aliakbar (UOCHB-X) ORCID
    Novotná, Barbora (UOCHB-X) ORCID
    Nencka, Radim (UOCHB-X) RID, ORCID
    Birkuš, Gabriel (UOCHB-X) ORCID
    Rulíšek, Lubomír (UOCHB-X) RID, ORCID
    Bouřa, Evžen (UOCHB-X) ORCID
    Source TitleAngewandte Chemie - International Edition. - : Wiley - ISSN 1433-7851
    Roč. 60, č. 18 (2021), s. 10172-10178
    Number of pages7 s.
    Languageeng - English
    CountryDE - Germany
    Keywordsconformational analysis ; cyclic dinucleotides ; entropy ; quantum chemistry ; strain energy
    OECD categoryPhysical chemistry
    R&D ProjectsGA20-08772S GA ČR - Czech Science Foundation (CSF)
    EF16_019/0000729 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 WOS000631782200001
    EID SCOPUS85103176233
    DOI10.1002/anie.202016805
    AnnotationSTING (stimulator of interferon genes) is a key regulator of innate immunity that has recently been recognized as a promising drug target. STING is activated by cyclic dinucleotides (CDNs) which eventually leads to expression of type I interferons and other cytokines. Factors underlying the affinity of various CDN analogues are poorly understood. Herein, we correlate structural biology, isothermal calorimetry (ITC) and computational modeling to elucidate factors contributing to binding of six CDNs—three pairs of natural (ribo) and fluorinated (2′‐fluororibo) 3′,3′‐CDNs. X‐ray structural analyses of six {STING:CDN} complexes did not offer any explanation for the different affinities of the studied ligands. ITC showed entropy/enthalpy compensation up to 25 kcal mol−1 for this set of similar ligands. The higher affinities of fluorinated analogues are explained with help of computational methods by smaller loss of entropy upon binding and by smaller strain (free) energy.
    WorkplaceInstitute of Organic Chemistry and Biochemistry
    Contactasep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418
    Year of Publishing2022
    Electronic addresshttps://doi.org/10.1002/anie.202016805
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