About: Protein-containing PEGylated cubosomic particles: freeze-fracture electron microscopy and synchrotron radiation circular dichroism study     Goto   Sponge   NotDistinct   Permalink

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  • 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)
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)
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)
skos:notation
  • RIV/61389013:_____/12:00378735!RIV13-AV0-61389013
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I, P(GAP208/10/1600), Z(AV0Z40500505)
http://linked.open...iv/cisloPeriodika
  • 26
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
  • Angelov, Borislav
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 163060
http://linked.open...ai/riv/idVysledku
  • RIV/61389013:_____/12:00378735
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • freeze-fracture electron microscopy; synchrotron radiation circular dichroism; SAXS (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [C69F53C4FD7E]
http://linked.open...i/riv/nazevZdroje
  • Journal of Physical Chemistry B
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 116
http://linked.open...iv/tvurceVysledku
  • Angelov, Borislav
  • Angelova, A.
  • Lesieur, S.
  • Nicolas, V.
  • Hoffmann, S. V.
  • Papahadjopoulos-Sternberg, B.
http://linked.open...ain/vavai/riv/wos
  • 000305933800009
http://linked.open...n/vavai/riv/zamer
issn
  • 1520-6106
number of pages
http://bibframe.org/vocab/doi
  • 10.1021/jp303863q
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