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Detection of globular and fibrillar proteins by quartz crystal microbalance sensor coated with a functionalized diamond thin film

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389021%3A_____%2F22%3A00561903" target="_blank" >RIV/61389021:_____/22:00561903 - isvavai.cz</a>

  • Nalezeny alternativní kódy

    RIV/68378271:_____/22:00561903 RIV/68407700:21230/22:00356717

  • Výsledek na webu

    <a href="https://doi.org/10.1016/j.apsusc.2022.153017" target="_blank" >https://doi.org/10.1016/j.apsusc.2022.153017</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.apsusc.2022.153017" target="_blank" >10.1016/j.apsusc.2022.153017</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Detection of globular and fibrillar proteins by quartz crystal microbalance sensor coated with a functionalized diamond thin film

  • Popis výsledku v původním jazyce

    This study presents a sensor based on quartz crystal microbalance (QCM) coated with nanocrystalline diamond (NCD) thin film, functionalization method and novel application of such sensor. Diamond-coated QCMs (DQCMs) were superficially terminated by hydrogen and oxygen (H-NCD and O-NCD) to control its surface dipole/po- tential. Two protein solutions were tested: bovine serum albumin (BSA) and fibronectin (FN). We performed reference measurements of serial resonant frequency (SRF) of clean QCMs loaded with protein and compared them with SRF shifts DQCMs loaded with proteins. In order to investigate the influence of the deposited NCD thin film on QCM measuring capabilities, additional FEM analysis was performed. The simulation results showed that QCM sensors maintain the sensing capabilities with a rigid thin film of NCD on its surface. The shift of SRF was demonstrably caused by the weight of protein adhered to the diamond film’s surface. We compared masses estimated from the Sauerbrey equation to characterize the adhesive properties of the studied proteins. Comparing bare QCM and DQCM, we discovered diamonds enhance the sensing performance for proteins. At the same time, it saturates quickly with phosphate buffer saline used as a diluent solution for proteins. Results showed a significant increase in protein adhesion confirmed by the increase of the mass for both oxygen and hydrogen-terminated DQCMs. Moreover, a different time-dependent behaviour (i.e. different adsorption rate, degrees of physisorption and/or preference of the diamond surface functionalization) of the O-NCD and H-NCD QCMs was observed for BSA and FN proteins. In this meaning, we propose a schematic model which describes the detection principle of BSA and FN proteins on H- and O-terminated DQCM sensors. Finally, a simple proof of concept for using the functionalized diamond-coated sensors with current stimulation and EQCM (Electro- chemical Quartz Crystal Microbalance) is also proposed.n

  • Název v anglickém jazyce

    Detection of globular and fibrillar proteins by quartz crystal microbalance sensor coated with a functionalized diamond thin film

  • Popis výsledku anglicky

    This study presents a sensor based on quartz crystal microbalance (QCM) coated with nanocrystalline diamond (NCD) thin film, functionalization method and novel application of such sensor. Diamond-coated QCMs (DQCMs) were superficially terminated by hydrogen and oxygen (H-NCD and O-NCD) to control its surface dipole/po- tential. Two protein solutions were tested: bovine serum albumin (BSA) and fibronectin (FN). We performed reference measurements of serial resonant frequency (SRF) of clean QCMs loaded with protein and compared them with SRF shifts DQCMs loaded with proteins. In order to investigate the influence of the deposited NCD thin film on QCM measuring capabilities, additional FEM analysis was performed. The simulation results showed that QCM sensors maintain the sensing capabilities with a rigid thin film of NCD on its surface. The shift of SRF was demonstrably caused by the weight of protein adhered to the diamond film’s surface. We compared masses estimated from the Sauerbrey equation to characterize the adhesive properties of the studied proteins. Comparing bare QCM and DQCM, we discovered diamonds enhance the sensing performance for proteins. At the same time, it saturates quickly with phosphate buffer saline used as a diluent solution for proteins. Results showed a significant increase in protein adhesion confirmed by the increase of the mass for both oxygen and hydrogen-terminated DQCMs. Moreover, a different time-dependent behaviour (i.e. different adsorption rate, degrees of physisorption and/or preference of the diamond surface functionalization) of the O-NCD and H-NCD QCMs was observed for BSA and FN proteins. In this meaning, we propose a schematic model which describes the detection principle of BSA and FN proteins on H- and O-terminated DQCM sensors. Finally, a simple proof of concept for using the functionalized diamond-coated sensors with current stimulation and EQCM (Electro- chemical Quartz Crystal Microbalance) is also proposed.n

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    30404 - Biomaterials (as related to medical implants, devices, sensors)

Návaznosti výsledku

  • Projekt

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

  • Návaznosti

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Ostatní

  • Rok uplatnění

    2022

  • Kód důvěrnosti údajů

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

Údaje specifické pro druh výsledku

  • Název periodika

    Applied Surface Science

  • ISSN

    0169-4332

  • e-ISSN

    1873-5584

  • Svazek periodika

    589

  • Číslo periodika v rámci svazku

    July

  • Stát vydavatele periodika

    NL - Nizozemsko

  • Počet stran výsledku

    8

  • Strana od-do

    153017

  • Kód UT WoS článku

    000780337200003

  • EID výsledku v databázi Scopus

    2-s2.0-85126027626