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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

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

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

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

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Applied Surface Science

  • ISSN

    0169-4332

  • e-ISSN

    1873-5584

  • Volume of the periodical

    589

  • Issue of the periodical within the volume

    July

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    8

  • Pages from-to

    153017

  • UT code for WoS article

    000780337200003

  • EID of the result in the Scopus database

    2-s2.0-85126027626