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  • Novel surface active maghemite nanoparticles (SAMNs) possessing peculiar colloidal properties and surface characteristics are able to covalently bind biomolecules. The interactions of SAMNs and rhodamine derivatized SAMNs (SAMN@RITC) with proteins from cell culture medium were studied by gel electrophoresis and mass spectrometry. Among the 3000 proteins present in fetal calf serum, SAMNs. and SAMN@RITC give rise to the formation of a self-assembled corona shell with 22 selected proteins, representing minor plasma proteins, among which alpha-2-HS- glycoprotein stands. out Bovine serum albumin: (BSA), representing 80% of the total serum proteins, shows negligible absorption on the SAMN surface: Nevertheless; SAMNs :. are able to bind BSA, upon incubation in pure BSA solutions The interaction between SAMNs and BSA was investigated by optical Spectroscopy, circular dichroism, Fourier transform infrared spectroscopy, and transmission electron microscopy. BSA binding resulted a time consuming process, nevertheless experimental results showed the interaction of 6 +/- 2 BSA molecules per nanoparticle, and optical Spectra indicate remarkable changes in SAMN optical features, as well as circular dichroism proved secondary structure alteration of bound BSA; suggesting that the protein needs to adapt its structure to adhere to nanoparticle surface. The selectively bound protein corona shell, formed upon SAMNs incubation in calf serum; was responsible for the characteristic behavior when SAMNs were tested for cell internalization and cytotoxicity on HeLa cells. Cytotoxicity of SAMN preparations Was extensively studied, and was negligible up to 100 mu g mL(-1). Moreover, nanoparticle uptake proceeded for long times, suggesting a correlation between internalization and stability of covalently bound self assembled protein corona, representing a. unique example of magnetic nanoparticle opsonization via covalent,:binding.
  • Novel surface active maghemite nanoparticles (SAMNs) possessing peculiar colloidal properties and surface characteristics are able to covalently bind biomolecules. The interactions of SAMNs and rhodamine derivatized SAMNs (SAMN@RITC) with proteins from cell culture medium were studied by gel electrophoresis and mass spectrometry. Among the 3000 proteins present in fetal calf serum, SAMNs. and SAMN@RITC give rise to the formation of a self-assembled corona shell with 22 selected proteins, representing minor plasma proteins, among which alpha-2-HS- glycoprotein stands. out Bovine serum albumin: (BSA), representing 80% of the total serum proteins, shows negligible absorption on the SAMN surface: Nevertheless; SAMNs :. are able to bind BSA, upon incubation in pure BSA solutions The interaction between SAMNs and BSA was investigated by optical Spectroscopy, circular dichroism, Fourier transform infrared spectroscopy, and transmission electron microscopy. BSA binding resulted a time consuming process, nevertheless experimental results showed the interaction of 6 +/- 2 BSA molecules per nanoparticle, and optical Spectra indicate remarkable changes in SAMN optical features, as well as circular dichroism proved secondary structure alteration of bound BSA; suggesting that the protein needs to adapt its structure to adhere to nanoparticle surface. The selectively bound protein corona shell, formed upon SAMNs incubation in calf serum; was responsible for the characteristic behavior when SAMNs were tested for cell internalization and cytotoxicity on HeLa cells. Cytotoxicity of SAMN preparations Was extensively studied, and was negligible up to 100 mu g mL(-1). Moreover, nanoparticle uptake proceeded for long times, suggesting a correlation between internalization and stability of covalently bound self assembled protein corona, representing a. unique example of magnetic nanoparticle opsonization via covalent,:binding. (en)
Title
  • Magnetic Nanoparticles with Covalently Bound Self-Assembled Protein Corona for Advanced Biomedical Applications
  • Magnetic Nanoparticles with Covalently Bound Self-Assembled Protein Corona for Advanced Biomedical Applications (en)
skos:prefLabel
  • Magnetic Nanoparticles with Covalently Bound Self-Assembled Protein Corona for Advanced Biomedical Applications
  • Magnetic Nanoparticles with Covalently Bound Self-Assembled Protein Corona for Advanced Biomedical Applications (en)
skos:notation
  • RIV/61989592:15310/13:33145789!RIV14-MSM-15310___
http://linked.open...avai/predkladatel
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(ED2.1.00/03.0058), P(EE2.3.20.0155)
http://linked.open...iv/cisloPeriodika
  • 39
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 85717
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/13:33145789
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • phagocytosis; nanotoxicology; binding; toxicity; adsorption; cells; drug-delivery; plasma-proteins; serum-albumin; iron-oxide nanoparticles (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [4E766F336BE3]
http://linked.open...i/riv/nazevZdroje
  • Journal of Physical Chemistry Part C: Nanomaterials and Interfaces
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
  • 117
http://linked.open...iv/tvurceVysledku
  • Zbořil, Radek
  • Baratella, Davide
  • Magro, Massimiliano
  • Vianello, Fabio
  • Miotto, Giovanni
  • Bonaiuto, Emanuela
  • Dallan, Marco
  • Venerando, Rina
http://linked.open...ain/vavai/riv/wos
  • 000326300700062
issn
  • 1932-7447
number of pages
http://bibframe.org/vocab/doi
  • 10.1021/jp4068137
http://localhost/t...ganizacniJednotka
  • 15310
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