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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 
Keywords: Botulinum neurotoxin A
Energy transfer
Exciton–plasmon interaction
Photoelectrochemical detection
Issue Date: 2018
Publisher: Elsevier
Source: Electrochemistry communications, 2018, v. 97, p. 114-118 How to cite?
Journal: Electrochemistry communications 
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.
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 (
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
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