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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/60461373:22340/20:43920772 RIV/67985858:_____/20:00541353

Výsledek na webu

<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>

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

International Journal of Pharmaceutics

ISSN

0378-5173

e-ISSN

—

Svazek periodika

2020

Číslo periodika v rámci svazku

579

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

"nestrankovano"

Kód UT WoS článku

000529310300037

EID výsledku v databázi Scopus

2-s2.0-85079904483