Magnetic Nanoparticles with Covalently Bound Self-Assembled Protein Corona for Advanced Biomedical Applications

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33145789" target="_blank" >RIV/61989592:15310/13:33145789 - isvavai.cz</a>

Výsledek na webu

<a href="http://pubs.acs.org/doi/ipdf/10.1021/jp4068137" target="_blank" >http://pubs.acs.org/doi/ipdf/10.1021/jp4068137</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jp4068137" target="_blank" >10.1021/jp4068137</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Magnetic Nanoparticles with Covalently Bound Self-Assembled Protein Corona for Advanced Biomedical Applications

Popis výsledku v původním jazyce

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 incubationin 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 consumin

Název v anglickém jazyce

Magnetic Nanoparticles with Covalently Bound Self-Assembled Protein Corona for Advanced Biomedical Applications

Popis výsledku anglicky

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 incubationin 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 consumin

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Physical Chemistry Part C: Nanomaterials and Interfaces

ISSN

1932-7447

e-ISSN

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Svazek periodika

117

Číslo periodika v rámci svazku

39

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

20320-20331

Kód UT WoS článku

000326300700062

EID výsledku v databázi Scopus

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