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Title: | A novel protein binding strategy for energy-transfer-based photoelectrochemical detection of enzymatic activity of Botulinum Neurotoxin A | Authors: | Lin, P Liu, D Wei, W Guo, J Ke, S Zeng, X Chen, S |
Issue Date: | 2018 | Source: | Electrochemistry communications, 2018, v. 97, p. 114-118 | Abstract: | In this work, we propose a novel energy-transfer-based photoelectrochemical (PEC) platform for probing of protein-protein interaction, which associates intimately with zinc-dependent cleavage and substrate specificities in the enzymatic activities of botulinum neurotoxin (BoNT). Specifically, by using substrate protein SNAP-25 as the energy-transfer nanoprobe, an exciton-plasmon interaction (EPI) based strategy between CdS quantum dots (QDs) and Au nanoparticles (NPs) in a PEC system is constructed with the photocurrent declining. Interestingly, the EPI effect is then interrupted by the target botulinum neurotoxin serotype A light chain (BoNT-LCA) special cleavage of the probe SNAP-25, leading to the photocurrent recovery. Therefore, the enzymatic activity of BoNT-LCA could be sensitively detected with a detection limit of 1 pg/mL. Unlike conventional DNA-programable assembly, a protein probe is used to bridge the excitons and plasmons in this work, which provides a new route for the investigation of the EPI-based bioassay. | Keywords: | Botulinum neurotoxin A CdS QDs Energy transfer Exciton–plasmon interaction Photoelectrochemical detection |
Publisher: | Elsevier | Journal: | Electrochemistry communications | ISSN: | 1388-2481 | EISSN: | 1873-1902 | DOI: | 10.1016/j.elecom.2018.11.004 | Rights: | © 2018 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license (http://creativecommons.org/licenses/BY-NC-ND/4.0/) The following publication: Lin, P., Liu, D., Wei, W., Guo, J., Ke, S., Zeng, X., & Chen, S. (2018). A novel protein binding strategy for energy-transfer-based photoelectrochemical detection of enzymatic activity of botulinum neurotoxin A. Electrochemistry Communications, 97, 114-118 is available at https://doi.org/10.1016/j.elecom.2018.11.004 |
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