Electrochemical biosensor based on three components random conjugated polymer with fullerene (C60)


KURBANOĞLU S., Cevher S. C. , TOPPARE L. K. , ÇIRPAN A., Soylemez S.

Bioelectrochemistry, vol.147, 2022 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 147
  • Publication Date: 2022
  • Doi Number: 10.1016/j.bioelechem.2022.108219
  • Journal Name: Bioelectrochemistry
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Chimica, Compendex, EMBASE, MEDLINE, Veterinary Science Database
  • Keywords: Catechol detection, Conjugated random polymer, Enzyme inhibition, Fullerene, Indomethacin, Tyrosinase
  • Middle East Technical University Affiliated: Yes

Abstract

© 2022 Elsevier B.V.Herein, a conjugated polymer and fullerene bearing architecture-based electrochemical Tyrosinase (Tyr) enzyme inhibition biosensor for indomethacin (INDO) drug active compound has been developed. For this purpose, three moieties of benzoxadiazole, thienopyrroledione, and benzodithiophene containing conjugated polymer; poly[BDT-alt-(TP;BO)] was used as a transducer modifier together with fullerene for catechol detection. The specific combination of these materials is considered an effective way to fabricate highly sensitive and fast response catechol biosensors for the first time. Electrochemical and surface characteristics of the modified electrodes were obtained by cyclic voltammetry, electrochemical impedance spectroscopy, scanning electron microscopy, and atomic force microscopy. The effect of the parameters during chronoamperometric measurements on the biosensor response was also studied. Using optimized conditions, biosensing of catechol was achieved between 0.5 and 62.5 µM with a limit of the detection 0.11 µM. Tyr inhibition was followed with INDO drug active compound and it was found that INDO has a mixed type characteristic of enzyme kinetics with an I50 value of 15.11 µM.