A novel protein binding strategy for energy-transfer-based photoelectrochemical detection of enzymatic activity of botulinum neurotoxin A
Research output: Journal Publications and Reviews (RGC: 21, 22, 62) › 21_Publication in refereed journal › peer-review
Author(s)
Detail(s)
Original language | English |
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Pages (from-to) | 114-118 |
Journal / Publication | Electrochemistry Communications |
Volume | 97 |
Online published | 13 Nov 2018 |
Publication status | Published - Dec 2018 |
Externally published | Yes |
Link(s)
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.
Research Area(s)
- Botulinum neurotoxin A, CdS QDs, Energy transfer, Exciton–plasmon interaction, Photoelectrochemical detection
Citation Format(s)
A novel protein binding strategy for energy-transfer-based photoelectrochemical detection of enzymatic activity of botulinum neurotoxin A. / Lin, Peng; Liu, Dan; Wei, Weiwei; Guo, Jiubiao; Ke, Shanming; Zeng, Xierong; Chen, Sheng.
In: Electrochemistry Communications, Vol. 97, 12.2018, p. 114-118.Research output: Journal Publications and Reviews (RGC: 21, 22, 62) › 21_Publication in refereed journal › peer-review