Plekhanov A. Yu.
1,2, Puzyk M. V.
3, Usikov A. S.
4,5, Roenkov A. D.6, Lebedev A. A.
5, Lebedev S. P.
7, Klotchenko S. A.
7, Vasin A. V.
7, Makarov Yu. N.
4
1Konstantinov Petersburg Nuclear Physics Institute, National Research Center Kurchatov Institute, Gatchina, Russia
2Institute of Macromolecular Compounds, Russian Academy of Sciences, St. Petersburg, Russia
3Herzen State Pedagogical University of Russia, St. Petersburg, Russia
4Nitride Crystals Inc., Richmond, USA
5Ioffe Institute, St. Petersburg, Russia
6Nitride Crystals Group, St. Petersburg, Russia
7Peter the Great Saint-Petersburg Polytechnic University, St. Petersburg, Russia
Email: puzyk@mail.ru, alexander.usikov@nitride-crystals.com
To analyze the modification of the functionalized surface of graphene by protein molecules, a chemiluminescent enzyme-linked immunosorbent assay based method was proposed. Using the example of functionalized graphene (FG) purification, the possibilities of chemiluminescent control of the state of its surface are shown. Methods for purifying FG from protein molecules with the restoration of the ability to resorb protein molecules are discussed. It has been shown that the FG surface can be cleaned from sorbed proteins, and a biosensor can be designed again based on such purified graphene, including with a different specificity. Therefore, the graphene sensor can be used repeatedly. Keywords: functionalized graphene, 1-pyrenemethylamine hydrochloride, cyclic voltammetry, chemiluminescence, monoclonal antibodies, biosensors
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