Glucose-modified carbosilane dendrimers: Interaction with model membranes and human serum albumin
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
32061725
DOI
10.1016/j.ijpharm.2020.119138
PII: S0378-5173(20)30122-8
Knihovny.cz E-resources
- Keywords
- Circular dichroism, Differential scanning calorimetry, Glucose-modified carbosilane dendrimers, Liposomes, Membrane fluidity, Model lipid membranes, Proteins,
- MeSH
- Circular Dichroism MeSH
- Dendrimers chemistry pharmacology MeSH
- Membrane Fluidity drug effects MeSH
- Spectrometry, Fluorescence MeSH
- Glucose chemistry pharmacology MeSH
- Hydrophobic and Hydrophilic Interactions MeSH
- Humans MeSH
- Serum Albumin, Human metabolism MeSH
- Liposomes MeSH
- Neoplasms drug therapy MeSH
- Drug Carriers chemistry pharmacology MeSH
- Antineoplastic Agents administration & dosage MeSH
- Silanes chemistry pharmacology MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- carbosilane MeSH Browser
- Dendrimers MeSH
- Glucose MeSH
- Serum Albumin, Human MeSH
- Liposomes MeSH
- Drug Carriers MeSH
- Antineoplastic Agents MeSH
- Silanes MeSH
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, DDM1-3Glu) 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 DDM2Glu, whereas DDM1Glu 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 DDM2-3Glu, significantly affect the type and extent of interaction with biological structures.
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