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Glucose-modified carbosilane dendrimers: Interaction with model membranes and human serum albumin.
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SYSNO ASEP 0541353 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Glucose-modified carbosilane dendrimers: Interaction with model membranes and human serum albumin. Author(s) 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)Article number 119138 Source Title International Journal of Pharmaceutics. - : Elsevier - ISSN 0378-5173
Roč. 579, APR 15 (2020)Number of pages 9 s. Language eng - English Country GB - United Kingdom Keywords glucose-modified carbosilane dendrimers ; liposomes ; model lipid membranes Subject RIV CC - Organic Chemistry OECD category Organic chemistry R&D Projects LTC19049 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support UCHP-M - RVO:67985858 UT WOS 000529310300037 EID SCOPUS 85079904483 DOI 10.1016/j.ijpharm.2020.119138 Annotation 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. Workplace Institute of Chemical Process Fundamentals Contact Eva Jirsová, jirsova@icpf.cas.cz, Tel.: 220 390 227 Year of Publishing 2022 Electronic address https://www.sciencedirect.com/science/article/pii/S0378517320301228?via%3Dihub
Number of the records: 1