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Function of thin film nanocrystalline diamond-protein SGFET independent of grain size

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378271%3A_____%2F12%3A00386606" target="_blank" >RIV/68378271:_____/12:00386606 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11110/12:12615

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.snb.2012.02.049" target="_blank" >http://dx.doi.org/10.1016/j.snb.2012.02.049</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.snb.2012.02.049" target="_blank" >10.1016/j.snb.2012.02.049</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Function of thin film nanocrystalline diamond-protein SGFET independent of grain size

  • Original language description

    We employ nanocrystalline diamond (NCD) thin films with average grain sizes of 250 and 80 nm to resolve influence of grain boundaries and sp2 phase on protein adsorption and electronic function of solutiongated field-effect transistors (SGFET). Microscopic (20 u m 60 um) SGFETs are fabricated without gate oxides based on hydrogen-terminated NCD films on glass substrates. We show that NCD with grain sizes down to 80 nm and film thickness of 100 nm is fully operational as SGFET. We find that inherent hysteresis of SGFET transfer characteristics, their reaction time, their negative shift after protein adsorption and cell culturing process, low gate leakage currents and no influence of UV sterilization or rinsing are all independent of the NCD grain size.Thus we propose a microscopic model where the function of NCD SGFET is determined by the H-terminated surface of diamond nanocrystals and its interaction with proteins, not by grain boundaries or sp2 phase in general.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    BM - Solid-state physics and magnetism

  • OECD FORD branch

Result continuities

  • Project

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

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2012

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Sensors and Actuators B - Chemical

  • ISSN

    0925-4005

  • e-ISSN

  • Volume of the periodical

    166-167

  • Issue of the periodical within the volume

    May

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    7

  • Pages from-to

    239-245

  • UT code for WoS article

    000305356900035

  • EID of the result in the Scopus database