Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/33811
Title: A reduced graphene oxide-Au based electrochemical biosensor for ultrasensitive detection of enzymatic activity of botulinum neurotoxin A
Authors: Chan, CY
Guo, J
Sun, C
Tsang, MK
Tian, F
Hao, J 
Chen, S 
Yang, M
Keywords: Botulinum neurotoxin type A (BoNT/A)
Differential pulse voltammetry (DPV)
Electrochemical biosensor
Reduced graphene oxide (rGO)
Issue Date: 2015
Publisher: Elsevier
Source: Sensors and actuators. B, Chemical, 2015, v. 220, p. 131-137 How to cite?
Journal: Sensors and actuators. B, Chemical 
Abstract: Botulinum neurotoxin serotype A (BoNT/A) is a type of neurotoxin which is able to cause fatal paralytic illness botulism in a low dosage. Therefore, there is a great need to develop an ultrasensitive bioassay to detect its active state for early diagnostics and prevention. This paper presents a reduced graphene oxide (rGO)/Au electrode based electrochemical biosensor for ultrasensitive detection of BoNT serotype A light chain (BoNT-LcA) protease activity. The fabricated rGO/Au electrode provides a robust and biocompatible platform with enhanced electron transfer capability and large area for peptide immobilization. SNAP-25-GFP peptide substrate is firstly immobilized on rGO surface via pyrenebutyric acid (PA) linker. The addition of BoNT-LcA could specifically cut SNAP-25-GFP at the cleavage sites to release the cut section from the electrode surface. This enzymatic activity of BoNT-LcA on SNAP-25-GFP peptide substrate could be detected by monitoring the enhanced redox probe transfer rate by differential pulse voltammetry (DPV) with a linear detection range from 1 pg/mL to 1 ng/mL and the limit of detection (LOD) for BoNT-LcA is around 8.6 pg/mL. The specificity of this biosensor is demonstrated with BoNT-LcB and heat-treated BoNT-LcA. Moreover, the experiments for BoNT-LcA detection in milk samples demonstrate the feasibility of this biosensor in complex matrix.
URI: http://hdl.handle.net/10397/33811
ISSN: 0925-4005
EISSN: 1873-3077
DOI: 10.1016/j.snb.2015.05.052
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