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Detection of protein adsorption by quartz crystal microbalance sensor coated by functionalized diamond film

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68407700%3A21110%2F16%3A00306333" target="_blank" >RIV/68407700:21110/16:00306333 - isvavai.cz</a>

  • Nalezeny alternativní kódy

    RIV/68407700:21230/16:00306333

  • Výsledek na webu

  • DOI - Digital Object Identifier

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Detection of protein adsorption by quartz crystal microbalance sensor coated by functionalized diamond film

  • Popis výsledku v původním jazyce

    The quartz crystal microbalance (QCM) is piezoelectric device capable of measuring mass changes in the nanogram range due to adsorbed macromolecules, nanoparticles, etc. Standard QCM’s are fabricated of a thin piezoelectric crystal plate with circular gold electrodes deposited on each side of the plate. To enhance sensitivity and selectivity to the monitored media various thin films were deposited on QCMs. In this study we present a sensor based on quartz crystal microbalance (QCM) piezoelectric device coated with functionalized nanocrystalline diamond (NCD) thin film. Diamond-coated QCMs (D-QCMs) were superficially terminated by hydrogen and oxygen (HNCD and ONCD). Three culture solutions were tested: Fetal bovine serum (FBS), bovine serum albumin (BSA) and fibronectin (FN). We performed reference measurements of serial resonant frequency (SRF) of clean D-QCMs and compare them with SRF shifts of D-QCM loaded with proteins. Solutions were applied on one side of D-QCMs followed by rinsing, drying and eventually measurement. Then, the sequence was repeated for the second side. The SFR shift was influenced by the mass of the protein, which adhered provably on the diamond surface. We compared these shifts to characterize adhesive properties of every individual protein solution. Results showed significant shifts for both by oxygen and hydrogen terminated D-QCMs in order of hundreds of Hz to lower frequencies (from –50 Hz to –643 Hz in SRF of rinsed clean sample). The highest shifts were observed for FBS, which is consistent with the theory, since it is compound of both BSA and FN. Comparing surface termination by oxygen and by hydrogen, significant difference is apparent with use of fibronectin. In this case, ONCD showed higher SRF shift compared to SRF shift measured on HNCD sample (–154 Hz on ONCD-QCM, compared to –50 Hz on HNCD-QCM). Thus ONCD-QCMs (hydrophilic) are more sensitive to fibronectin, than HNCD-QCMs (hydrophobic).

  • Název v anglickém jazyce

    Detection of protein adsorption by quartz crystal microbalance sensor coated by functionalized diamond film

  • Popis výsledku anglicky

    The quartz crystal microbalance (QCM) is piezoelectric device capable of measuring mass changes in the nanogram range due to adsorbed macromolecules, nanoparticles, etc. Standard QCM’s are fabricated of a thin piezoelectric crystal plate with circular gold electrodes deposited on each side of the plate. To enhance sensitivity and selectivity to the monitored media various thin films were deposited on QCMs. In this study we present a sensor based on quartz crystal microbalance (QCM) piezoelectric device coated with functionalized nanocrystalline diamond (NCD) thin film. Diamond-coated QCMs (D-QCMs) were superficially terminated by hydrogen and oxygen (HNCD and ONCD). Three culture solutions were tested: Fetal bovine serum (FBS), bovine serum albumin (BSA) and fibronectin (FN). We performed reference measurements of serial resonant frequency (SRF) of clean D-QCMs and compare them with SRF shifts of D-QCM loaded with proteins. Solutions were applied on one side of D-QCMs followed by rinsing, drying and eventually measurement. Then, the sequence was repeated for the second side. The SFR shift was influenced by the mass of the protein, which adhered provably on the diamond surface. We compared these shifts to characterize adhesive properties of every individual protein solution. Results showed significant shifts for both by oxygen and hydrogen terminated D-QCMs in order of hundreds of Hz to lower frequencies (from –50 Hz to –643 Hz in SRF of rinsed clean sample). The highest shifts were observed for FBS, which is consistent with the theory, since it is compound of both BSA and FN. Comparing surface termination by oxygen and by hydrogen, significant difference is apparent with use of fibronectin. In this case, ONCD showed higher SRF shift compared to SRF shift measured on HNCD sample (–154 Hz on ONCD-QCM, compared to –50 Hz on HNCD-QCM). Thus ONCD-QCMs (hydrophilic) are more sensitive to fibronectin, than HNCD-QCMs (hydrophobic).

Klasifikace

  • Druh

    O - Ostatní výsledky

  • CEP obor

    BO - Biofyzika

  • OECD FORD obor

Návaznosti výsledku

  • Projekt

  • Návaznosti

    S - Specificky vyzkum na vysokych skolach

Ostatní

  • Rok uplatnění

    2016

  • Kód důvěrnosti údajů

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