A simple enzyme-catalyzed reaction induced "switch" type fluorescence biosensor based on carbon nitride nanosheets for the assay of alkaline phosphatase activity
An enzyme-catalyzed fluorescence "switch" type sensor was constructed for the determination of alkaline phosphatase (ALP) activity by combining the fluorescence quenching effect of Ag + on ultrathin g-C 3 N 4 nanosheets (CNNSs) with the simple redox reaction of AA and Ag + . Briefly, Ag +...
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Published in | Analyst (London) Vol. 145; no. 19; pp. 6277 - 6282 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Royal Society of Chemistry
28.09.2020
|
Subjects | |
Online Access | Get full text |
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Summary: | An enzyme-catalyzed fluorescence "switch" type sensor was constructed for the determination of alkaline phosphatase (ALP) activity by combining the fluorescence quenching effect of Ag
+
on ultrathin g-C
3
N
4
nanosheets (CNNSs) with the simple redox reaction of AA and Ag
+
. Briefly, Ag
+
exhibits a significant quenching effect on the fluorescence of CNNSs. Thus the fluorescence signal of the CNNS-Ag
+
system is extremely weak even in the presence of
l
-ascorbic acid-2-phosphate (AAP) ("off" state). When ALP coexists in the system, the enzyme can specifically catalyze the hydrolysis of AAP to form ascorbic acid (AA), which reduces Ag
+
to Ag
0
. In this case, the fluorescence signal of the system is recovered ("on" state). Based on this principle, a signal-enhanced CNNS fluorescence sensor was developed to determine the activity of alkaline phosphatase. The experimental results show that the detection range of alkaline phosphatase is 0.5-20 U L
−1
, and the detection limit is 0.05 U L
−1
(S/N = 3). Meanwhile, this method was used to assay ALP in serum samples.
An enzyme-catalyzed fluorescence "switch" type sensor was constructed for assay of alkaline phosphatase activity by combining the fluorescence quenching effect of Ag
+
on ultrathin g-C
3
N
4
nanosheets with the simple redox reaction of AA and Ag
+
. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0003-2654 1364-5528 |
DOI: | 10.1039/d0an01224f |