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Glucose-modified carbosilane dendrimers: Interaction with model membranes and human serum albumin.

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985858%3A_____%2F20%3A00541353" target="_blank" >RIV/67985858:_____/20:00541353 - isvavai.cz</a>

  • Nalezeny alternativní kódy

    RIV/44555601:13440/20:43895475 RIV/60461373:22340/20:43920772

  • Výsledek na webu

    <a href="https://www.sciencedirect.com/science/article/pii/S0378517320301228?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0378517320301228?via%3Dihub</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.ijpharm.2020.119138" target="_blank" >10.1016/j.ijpharm.2020.119138</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Glucose-modified carbosilane dendrimers: Interaction with model membranes and human serum albumin.

  • Popis výsledku v původním jazyce

    Glycodendrimers are a novel group of dendrimers (DDMs) characterized by surface modifications with various types of glycosides. It has been shown previously that such modifications significantly decrease the cytotoxicity of DDMs. Here, we present an investigation of glucose-modified carbosilane DDMs (first-third-generation, DDM(1-3)Glu) interactions with two models of biological structures: lipid membranes (liposomes) and serum protein (human serum albumin, HSA). The changes in lipid membrane fluidity with increasing concentration of DDMs was monitored by spectrofluorimetry and calorimetry methods. The influence of glycodendrimers on serum protein was investigated by monitoring changes in protein fluorescence intensity (fluorescence quenching) and as protein secondary structure alterations by circular dichroism spectrometry. Generally, all generations of DDMGlu induced a decrease of membrane fluidity and interacted weakly with HSA. Interestingly, in contrast to other dendritic type polymers, the extent of the DDM interaction with both biological models was not related to DDM generation. The most significant interaction with protein was shown in the case of DDM(2)Glu, whereas DDM(1)Glu induced the highest number of changes in membrane fluidity. In conclusion, our results suggest that the flexibility of a DDM molecule, as well as its typical structure (hydrophobic interior and hydrophilic surface) along with the formation of larger aggregates of DDM(2-3)Glu, significantly affect the type and extent of interaction with biological structures.

  • Název v anglickém jazyce

    Glucose-modified carbosilane dendrimers: Interaction with model membranes and human serum albumin.

  • Popis výsledku anglicky

    Glycodendrimers are a novel group of dendrimers (DDMs) characterized by surface modifications with various types of glycosides. It has been shown previously that such modifications significantly decrease the cytotoxicity of DDMs. Here, we present an investigation of glucose-modified carbosilane DDMs (first-third-generation, DDM(1-3)Glu) interactions with two models of biological structures: lipid membranes (liposomes) and serum protein (human serum albumin, HSA). The changes in lipid membrane fluidity with increasing concentration of DDMs was monitored by spectrofluorimetry and calorimetry methods. The influence of glycodendrimers on serum protein was investigated by monitoring changes in protein fluorescence intensity (fluorescence quenching) and as protein secondary structure alterations by circular dichroism spectrometry. Generally, all generations of DDMGlu induced a decrease of membrane fluidity and interacted weakly with HSA. Interestingly, in contrast to other dendritic type polymers, the extent of the DDM interaction with both biological models was not related to DDM generation. The most significant interaction with protein was shown in the case of DDM(2)Glu, whereas DDM(1)Glu induced the highest number of changes in membrane fluidity. In conclusion, our results suggest that the flexibility of a DDM molecule, as well as its typical structure (hydrophobic interior and hydrophilic surface) along with the formation of larger aggregates of DDM(2-3)Glu, significantly affect the type and extent of interaction with biological structures.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10401 - Organic chemistry

Návaznosti výsledku

  • Projekt

    <a href="/cs/project/LTC19049" target="_blank" >LTC19049: Charakterizace biologických vlastností karbosilanových dendrimerů a jejich potenciální využití v oblasti nádorové terapie</a><br>

  • Návaznosti

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

Ostatní

  • Rok uplatnění

    2020

  • Kód důvěrnosti údajů

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

Údaje specifické pro druh výsledku

  • Název periodika

    International Journal of Pharmaceutics

  • ISSN

    0378-5173

  • e-ISSN

    1873-3476

  • Svazek periodika

    579

  • Číslo periodika v rámci svazku

    APR 15

  • Stát vydavatele periodika

    GB - Spojené království Velké Británie a Severního Irska

  • Počet stran výsledku

    9

  • Strana od-do

    119138

  • Kód UT WoS článku

    000529310300037

  • EID výsledku v databázi Scopus

    2-s2.0-85079904483