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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

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

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • 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

    10401 - Organic chemistry

Result continuities

  • Project

    <a href="/en/project/LTC19049" target="_blank" >LTC19049: Characterization of biological properties of carbosilane dendrimers potentially used in the area of cancer treatment</a><br>

  • Continuities

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

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    International Journal of Pharmaceutics

  • ISSN

    0378-5173

  • e-ISSN

    1873-3476

  • Volume of the periodical

    579

  • Issue of the periodical within the volume

    APR 15

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    9

  • Pages from-to

    119138

  • UT code for WoS article

    000529310300037

  • EID of the result in the Scopus database

    2-s2.0-85079904483