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rdf:type
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Description
| - The entrapment of protein molecules in cubosomic nanocarriers that are sterically stabilized by an amphiphilic poly(ethylene glycol) (PEG) derivative are investigated. The mechanism of fragmentation of a self-assembled PEGylated cubic lipid phase into nanoparticles (NPs) is studied in excess aqueous medium. The molar ratio between the cubic-phase-forming lipid monoolein (MO) and its PEGylated derivative (MOPEG2000) is selected as to favor the formation of inverted-type liquid-crystalline (LC) structures. Freeze-fracture electron microscopy (FF-EM), quasi-elastic light scattering (QELS), confocal laser scanning fluorescence microscopy (CLSFM) and far-UV synchrotron radiation circular dichroism (SRCD) spectroscopy are applied for determination of the NPs' sizes, inner organization, stability, and interaction with the protein α-chymotrypsinogen A. The PEGylated cubosomes offer new possibilities for investigation of protein loading in sterically stabilized (“Stealth) lipid carriers.
- The entrapment of protein molecules in cubosomic nanocarriers that are sterically stabilized by an amphiphilic poly(ethylene glycol) (PEG) derivative are investigated. The mechanism of fragmentation of a self-assembled PEGylated cubic lipid phase into nanoparticles (NPs) is studied in excess aqueous medium. The molar ratio between the cubic-phase-forming lipid monoolein (MO) and its PEGylated derivative (MOPEG2000) is selected as to favor the formation of inverted-type liquid-crystalline (LC) structures. Freeze-fracture electron microscopy (FF-EM), quasi-elastic light scattering (QELS), confocal laser scanning fluorescence microscopy (CLSFM) and far-UV synchrotron radiation circular dichroism (SRCD) spectroscopy are applied for determination of the NPs' sizes, inner organization, stability, and interaction with the protein α-chymotrypsinogen A. The PEGylated cubosomes offer new possibilities for investigation of protein loading in sterically stabilized (“Stealth) lipid carriers. (en)
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Title
| - Protein-containing PEGylated cubosomic particles: freeze-fracture electron microscopy and synchrotron radiation circular dichroism study
- Protein-containing PEGylated cubosomic particles: freeze-fracture electron microscopy and synchrotron radiation circular dichroism study (en)
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skos:prefLabel
| - Protein-containing PEGylated cubosomic particles: freeze-fracture electron microscopy and synchrotron radiation circular dichroism study
- Protein-containing PEGylated cubosomic particles: freeze-fracture electron microscopy and synchrotron radiation circular dichroism study (en)
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skos:notation
| - RIV/61389013:_____/12:00378735!RIV13-AV0-61389013
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
| - I, P(GAP208/10/1600), Z(AV0Z40500505)
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/61389013:_____/12:00378735
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - freeze-fracture electron microscopy; synchrotron radiation circular dichroism; SAXS (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
| - Journal of Physical Chemistry B
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Angelov, Borislav
- Angelova, A.
- Lesieur, S.
- Nicolas, V.
- Hoffmann, S. V.
- Papahadjopoulos-Sternberg, B.
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http://linked.open...ain/vavai/riv/wos
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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http://bibframe.org/vocab/doi
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