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Targeting the insulin receptor with hormone and peptide dimers

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15640%2F22%3A73618689" target="_blank" >RIV/61989592:15640/22:73618689 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388963:_____/23:00564527 RIV/00216208:11310/23:10464279

  • Result on the web

    <a href="https://onlinelibrary.wiley.com/doi/10.1002/psc.3461" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1002/psc.3461</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/psc.3461" target="_blank" >10.1002/psc.3461</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Targeting the insulin receptor with hormone and peptide dimers

  • Original language description

    Insulin is a key hormone involved in the regulation of overall energetic homeostasis of the organism. The dimeric character of the receptor for insulin evokes ideas about its activation or inhibition with peptide dimers that could either trigger or block the structural transition of the insulin receptor, leading to its activation. Herewith, we present the chemical engineering and biological characterization of several series of insulin dimers or dimers of specific peptides that should be able to bind receptors for insulin or insulin growth factor 1. The hormones or peptides in the dimers were interconnected with different linkers, consisting of triazole moieties and 3, 6, 8, 11, or 23 polyethylene glycol units. The prepared dimers were weaker in binding to insulin receptors than human insulin. However, some of the insulin dimers showed preferential binding specificity toward the isoform A of the insulin receptor, and the insulin dimers also stimulated the insulin receptor more strongly than would be consistent with their binding affinities. Our results suggest that designing insulin dimers may be a promising strategy for modulating the ability of the hormone to activate the receptor or to alter its specificity toward insulin receptor isoforms.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    21002 - Nano-processes (applications on nano-scale); (biomaterials to be 2.9)

Result continuities

  • Project

    <a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    JOURNAL OF PEPTIDE SCIENCE

  • ISSN

    1075-2617

  • e-ISSN

    1099-1387

  • Volume of the periodical

    29

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    9

  • Pages from-to

    "nečíslováno"

  • UT code for WoS article

    000883179300001

  • EID of the result in the Scopus database

    2-s2.0-85142158035