Journal
TALANTA
Volume 147, Issue -, Pages 63-68Publisher
ELSEVIER
DOI: 10.1016/j.talanta.2015.09.033
Keywords
Trypsin; Chemiluminescence; Resonance energy transfer; Gold nanoclusters
Categories
Funding
- Fundamental Research Funds for the Central Universities [xjj2015121]
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A chemiluminescence resonance energy transfer (CRET) platform was developed for sensitive and label-free detection of protease by using trypsin as a model analyte. In this CRET platform, bis(2,4,6-trichlorophenyl)oxalate-hydrogen peroxide chemiluminescence (CL) reaction was utilized as an energy donor and bovine serum albumin (BSA)-stabilized gold nanoclusters (Au NCs) as an energy acceptor. The BSA-stabilized Au NCs triggered the CRET phenomenon by accepting the energy from TCPO-H2O2 CL reaction, thus producing intense CL. In the presence of trypsin, the protein template of BSA-stabilized Au NCs was digested, which frustrated the energy transfer efficiency between the CL donor and the BSA-stabilized Au NCs, leading to a significant decrease in the CL signal. The decreased CL signal was proportional to the logarithm of trypsin concentration in the range of 0.01-50.0 mu g mL(-1). The detection limit for trypsin was 9 ng mL(-1) and the relative standard deviations were lesser than 3% (n=11). This Au NCs-based CRET platform was successfully applied to the determination of trypsin in human urine samples, demonstrating its potential application in clinical diagnosis. (C) 2015 Elsevier B.V. All rights reserved.
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