| Title : Selective and sensitive detection of acetylcholinesterase activity using denatured protein-protected gold nanoclusters as a label-free probe - Li_2014_Analyst_139_285 |
| Author(s) : Li H , Guo Y , Xiao L , Chen B |
| Ref : Analyst , 139 :285 , 2014 |
|
Abstract :
Based on the fluorescence quenching of novel denatured protein-protected gold nanoclusters, a label-free detection method of acetylcholinesterase (AChE) activity has been developed. Using denatured bovine serum albumin (dBSA), in which 35 cysteine residues can interact polyvalently with Au nanoclusters (AuNCs) as a stabilizing agent, water-soluble and stable fluorescent gold nanoclusters were synthesized. The fluorescence of the AuNCs was quenched by thiocholine that was produced from the AChE hydrolysis of S-acetylthiocholine iodide (ACTI) to detect the AChE activity. The linear range of the method was 0.005-0.15 U mL(-1). The limit of detection (LOD) was 0.02 mU mL(-1). Other enzymes and metal ions, i.e., GPT, gamma-GT, GOx, K(+), Ca(2+) and Na(+), showed minimal interference. Using the fluorescence probe, satisfactory results for the detection of the AChE activity in human serum were obtained. |
| PubMedSearch : Li_2014_Analyst_139_285 |
| PubMedID: 24251311 |
Li H, Guo Y, Xiao L, Chen B (2014)
Selective and sensitive detection of acetylcholinesterase activity using denatured protein-protected gold nanoclusters as a label-free probe
Analyst
139 :285
Li H, Guo Y, Xiao L, Chen B (2014)
Analyst
139 :285