Number of the records: 1  

Multipodal insulin mimetics built on adamantane or proline scaffolds

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    SYSNO ASEP0539200
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleMultipodal insulin mimetics built on adamantane or proline scaffolds
    Author(s) Hajduch, Jan (UOCHB-X) RID
    Fabre, Benjamin (UOCHB-X) ORCID
    Klopp, Benjamin (UOCHB-X)
    Pohl, Radek (UOCHB-X) RID, ORCID
    Buděšínský, Miloš (UOCHB-X) RID, ORCID
    Šolínová, Veronika (UOCHB-X) RID, ORCID
    Kašička, Václav (UOCHB-X) RID, ORCID
    Köprülüoglu, Cemal (UOCHB-X) ORCID, RID
    Eyrilmez, Saltuk M. (UOCHB-X) ORCID, RID
    Lepšík, Martin (UOCHB-X) RID, ORCID
    Hobza, Pavel (UOCHB-X) RID, ORCID
    Mitrová, Katarína (UOCHB-X)
    Lubos, Marta (UOCHB-X) ORCID
    Garre Hernández, María Soledad (UOCHB-X) ORCID
    Jiráček, Jiří (UOCHB-X) RID, ORCID
    Article number104548
    Source TitleBioorganic Chemistry. - : Elsevier - ISSN 0045-2068
    Roč. 107, Feb (2021)
    Number of pages17 s.
    Languageeng - English
    CountryUS - United States
    Keywordsinsulin receptor ; peptidomimetics ; scaffold ; solid-phase peptide synthesis ; hormone binding ; molecular dynamics
    OECD categoryOrganic chemistry
    R&D ProjectsEF16_019/0000729 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Method of publishingLimited access
    Institutional supportUOCHB-X - RVO:61388963
    UT WOS000618103400002
    EID SCOPUS85098193633
    DOI10.1016/j.bioorg.2020.104548
    AnnotationMulti-orthogonal molecular scaffolds can be applied as core structures of bioactive compounds. Here, we prepared four tri-orthogonal scaffolds based on adamantane or proline skeletons. The scaffolds were used for the solid-phase synthesis of model insulin mimetics bearing two different peptides on the scaffolds. We found that adamantane-derived compounds bind to the insulin receptor more effectively (Kd value of 0.5 μM) than proline-derived compounds (Kd values of 15–38 μM) bearing the same peptides. Molecular dynamics simulations suggest that spacers between peptides and central scaffolds can provide greater flexibility that can contribute to increased binding affinity. Molecular modeling showed possible binding modes of mimetics to the insulin receptor. Our data show that the structure of the central scaffold and flexibility of attached peptides in this type of compound are important and that different scaffolds should be considered when designing peptide hormone mimetics.
    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/10.1016/j.bioorg.2020.104548
Number of the records: 1  

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