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%2F44555601%3A13440%2F20%3A43895475" target="_blank" >RIV/44555601:13440/20:43895475 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22340/20:43920772 RIV/67985858:_____/20:00541353
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0378517320301228" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0378517320301228</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
10610 - Biophysics
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
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
—
Volume of the periodical
2020
Issue of the periodical within the volume
579
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
9
Pages from-to
"nestrankovano"
UT code for WoS article
000529310300037
EID of the result in the Scopus database
2-s2.0-85079904483