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Targeting galectin-4 with glycoconjugates of varying architectures: a multivalency étude with accent on anti-tumor effect and protection against apoptosis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00639544" target="_blank" >RIV/61388963:_____/25:00639544 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/25:00639544 RIV/68407700:21460/25:00389989 RIV/00216208:11310/25:10503720

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0223523425009146?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0223523425009146?via%3Dihub</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.ejmech.2025.118149" target="_blank" >10.1016/j.ejmech.2025.118149</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Targeting galectin-4 with glycoconjugates of varying architectures: a multivalency étude with accent on anti-tumor effect and protection against apoptosis

  • Original language description

    Galectin-4 (Gal-4) is a protumorigenic protein that strongly participates especially in gastrointestinal cancer and is increasingly recognized as a therapeutic target in gastrointestinal malignancies, where its dysregulated expression contributes to tumor progression and immune modulation. Its abundance and the extent of its involvement in these pathologies are comparable with its much better-studied counterparts, galectin-1 and3. However, to date, no systematic effort has been made to design efficient defined Gal-4 inhibitors with a potential therapeutic effect. In this work, we present a library of biocompatible multivalent Gal-4 inhibitors with diverse architectures to investigate how different modes of multivalent presentation of a common ligand, lactose, influence the binding affinity to Gal-4. The most efficient scaffold was then loaded with a high-affinity tetrasaccharide ligand of Gal-4, derived from lacto-N-tetraose, to further enhance Gal-4 binding. The resulting glycopolymer exhibited outstanding performance in inhibiting Gal-4-induced apoptosis of T lymphocytes, and, in addition, it efficiently scavenged Gal-4 from the surface of cancer cells. Both of these processes are relevant for tumor immune evasion. Given the high biocompatibility, and low toxicity of the POx carrier, this glycopolymer has a strong potential as a candidate for further development of glycotherapeutics against Gal-4-associated diseases such as gastrointestinal cancer.

  • 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

    10406 - Analytical chemistry

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    European Journal of Medicinal Chemistry

  • ISSN

    0223-5234

  • e-ISSN

    1768-3254

  • Volume of the periodical

    300

  • Issue of the periodical within the volume

    15 Dec

  • Country of publishing house

    FR - FRANCE

  • Number of pages

    12

  • Pages from-to

    118149

  • UT code for WoS article

    001583014200001

  • EID of the result in the Scopus database

    2-s2.0-105015645847