Journal
COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 103, Issue -, Pages 624-629Publisher
ELSEVIER
DOI: 10.1016/j.colsurfb.2012.08.039
Keywords
Carbon nanotubes; Covalent binding; Acetilcholinesterase; FT-IR; Cyclic voltammetry; EIS; Computational docking
Funding
- CAPES [PNPD/CAPES 0316083]
- National Science Foundation [OISE 0965814]
- Office Of Internatl Science &Engineering
- Office Of The Director [0965911] Funding Source: National Science Foundation
- Office Of The Director
- Office Of Internatl Science &Engineering [0965814] Funding Source: National Science Foundation
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This manuscript describes results related to the characterization of electrodes modified with a composite of acetylcholinesterase covalently bound to carbon nanotubes (CNT). The characterization was performed by computational methods and complemented by cyclic voltammetry, infrared spectroscopy, and electrochemical impedance spectroscopy. In-silico simulations enabled the identification of the binding site and the calculation of the interaction energy. Besides complementing the computational studies, experimental results obtained by cyclic voltammetry showed that the addition of CNT to the surface of electrodes yielded significant increases in effective area and greatly facilitated the electron transfer reactions. These results are also in agreement with impedance spectroscopy data, which indicated a high apparent rate constant, even after the immobilization of the enzyme. These results lend new information about the physical and chemical properties of biointerfaces at the molecular level, specifically about the mechanism and consequences of the interaction of a model enzyme with CNT. (C) 2012 Elsevier B.V. All rights reserved.
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