Počet záznamů: 1
Glucose-modified carbosilane dendrimers: Interaction with model membranes and human serum albumin.
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SYSNO ASEP 0541353 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Glucose-modified carbosilane dendrimers: Interaction with model membranes and human serum albumin. Tvůrce(i) Wróbel, D. (CZ)
Müllerová, Monika (UCHP-M) RID, ORCID, SAI
Strašák, Tomáš (UCHP-M) RID, ORCID, SAI
Růžička, K. (CZ)
Fulem, M. (CZ)
Kubíková, R. (CZ)
Bryszewska, M. (PL)
Klajnert-Maculewicz, B. (PL)
Malý, J. (CZ)Číslo článku 119138 Zdroj.dok. International Journal of Pharmaceutics. - : Elsevier - ISSN 0378-5173
Roč. 579, APR 15 (2020)Poč.str. 9 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova glucose-modified carbosilane dendrimers ; liposomes ; model lipid membranes Vědní obor RIV CC - Organická chemie Obor OECD Organic chemistry CEP LTC19049 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Open access Institucionální podpora UCHP-M - RVO:67985858 UT WOS 000529310300037 EID SCOPUS 85079904483 DOI 10.1016/j.ijpharm.2020.119138 Anotace 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. Pracoviště Ústav chemických procesů Kontakt Eva Jirsová, jirsova@icpf.cas.cz, Tel.: 220 390 227 Rok sběru 2022 Elektronická adresa https://www.sciencedirect.com/science/article/pii/S0378517320301228?via%3Dihub
Počet záznamů: 1