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 journalpeer-review

4 Scopus Citations
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Author(s)

  • Peng Lin
  • Dan Liu
  • Weiwei Wei
  • Jiubiao Guo
  • Shanming Ke
  • Xierong Zeng

Detail(s)

Original languageEnglish
Pages (from-to)114-118
Journal / PublicationElectrochemistry Communications
Volume97
Online published13 Nov 2018
Publication statusPublished - Dec 2018
Externally publishedYes

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 journalpeer-review