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Development of lectin arrays for mapping the glycosylations of proteins and cells

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F23%3A00132291" target="_blank" >RIV/00216224:14310/23:00132291 - isvavai.cz</a>

  • Výsledek na webu

  • DOI - Digital Object Identifier

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Development of lectin arrays for mapping the glycosylations of proteins and cells

  • Popis výsledku v původním jazyce

    Saccharides are essential for life, and in addition to their traditional roles as structural and energy storage components, they play crucial roles in many recognition events, signaling, and communication processes [1]. The glycosylation of cells reflects the biological species, tissue, developmental and physiological state of the organism. Importantly, changes in glycosylation patterns were observed in various tumors, and the aberrant glycosylation is often associated with malignancy potential, tumor immune surveillance, and patients´ prognosis [2]. Lectin arrays are widely used tools for analyzing glycosylation of various samples. They utilize a panel of lectins (saccharide-binding proteins with distinct sugar specificities) immobilized onto a solid surface. Lectin arrays allow for rapid and high-throughput glycomic analysis with minimal sample consumption. They can be used for glycan profiling of purified glycoproteins, cell/tissue lysates, membrane vesicles, complex biological samples, prokaryotic and eukaryotic cells. This talk will present the development of a customized lectin array in the microscope slide format. The microarrays are prepared by non-contact piezo dispensing of lectins onto a functionalized glass slide and their immobilization using various surface chemistries (immobilization on epoxy groups, NHS/EDC coupling). Fluorescence measurement is used to detect the binding of the glycosylated samples. The fabricated lectin arrays will be used, e.g., to map the glycosylation changes at different stages of cell differentiation or under different physiopathological conditions. [1] Zhan X, Dravid G, Ye Z, Hammond H, Shamblott M, Gearhart J, Cheng L. Lancet. 2004 [2] Mazalovska M, Kouokam JC. Biomed Res Int. 2020.

  • Název v anglickém jazyce

    Development of lectin arrays for mapping the glycosylations of proteins and cells

  • Popis výsledku anglicky

    Saccharides are essential for life, and in addition to their traditional roles as structural and energy storage components, they play crucial roles in many recognition events, signaling, and communication processes [1]. The glycosylation of cells reflects the biological species, tissue, developmental and physiological state of the organism. Importantly, changes in glycosylation patterns were observed in various tumors, and the aberrant glycosylation is often associated with malignancy potential, tumor immune surveillance, and patients´ prognosis [2]. Lectin arrays are widely used tools for analyzing glycosylation of various samples. They utilize a panel of lectins (saccharide-binding proteins with distinct sugar specificities) immobilized onto a solid surface. Lectin arrays allow for rapid and high-throughput glycomic analysis with minimal sample consumption. They can be used for glycan profiling of purified glycoproteins, cell/tissue lysates, membrane vesicles, complex biological samples, prokaryotic and eukaryotic cells. This talk will present the development of a customized lectin array in the microscope slide format. The microarrays are prepared by non-contact piezo dispensing of lectins onto a functionalized glass slide and their immobilization using various surface chemistries (immobilization on epoxy groups, NHS/EDC coupling). Fluorescence measurement is used to detect the binding of the glycosylated samples. The fabricated lectin arrays will be used, e.g., to map the glycosylation changes at different stages of cell differentiation or under different physiopathological conditions. [1] Zhan X, Dravid G, Ye Z, Hammond H, Shamblott M, Gearhart J, Cheng L. Lancet. 2004 [2] Mazalovska M, Kouokam JC. Biomed Res Int. 2020.

Klasifikace

  • Druh

    O - Ostatní výsledky

  • CEP obor

  • OECD FORD obor

    10609 - Biochemical research methods

Návaznosti výsledku

  • Projekt

    <a href="/cs/project/LM2023042" target="_blank" >LM2023042: Česká infrastruktura pro integrativní strukturní biologii</a><br>

  • Návaznosti

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Ostatní

  • Rok uplatnění

    2023

  • Kód důvěrnosti údajů

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