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“Light-up” Sensing of human 8-oxoguanine DNA glycosylase activity by target-induced autocatalytic DNAzyme-generated rolling circle amplification

Human 8-oxoguanine DNA glycosylase (hOGG1) plays a crucial role in maintaining the genomic integrity of living organisms for its capability of repairing DNA oxidative damage. The expression level of hOGG1 is closely associated with many diseases including various kinds of cancers. In this study, a n...

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Bibliographic Details
Published in:Biosensors & bioelectronics 2016-05, Vol.79, p.679-684
Main Authors: Kong, Xiang-Juan, Wu, Shuang, Cen, Yao, Yu, Ru-Qin, Chu, Xia
Format: Article
Language:English
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Summary:Human 8-oxoguanine DNA glycosylase (hOGG1) plays a crucial role in maintaining the genomic integrity of living organisms for its capability of repairing DNA oxidative damage. The expression level of hOGG1 is closely associated with many diseases including various kinds of cancers. In this study, a novel “light-up” sensor based on target-induced formation of 5′ phosphorylated probe and autocatalytic DNAzyme-generated rolling circle amplification has been developed for highly sensitive human 8-oxoguanine DNA glycosylase (hOGG1) activity assay. The approach reaches detection limit as low as 0.001U/mL for hOGG1 via scarcely increased background signal and dual signal amplification strategy. To the best of our knowledge, it is one of the most sensitive methods for the detection of base excision repair enzyme. Moreover, the approach shows excellent specificity over other nonspecific enzymes would interfere with the assay and holds great promise for application in real sample analysis. Hence, the proposed method provides a highly sensitive, selective, and desirable hOGG1 sensing platform. •A novel "light-up" sensor for human 8-oxoguanine DNA glycosylase activity assay was developed.•The work mainly relies on target-induced formation of 5′ phosphorylated probe and autocatalytic DNAzyme-generated rolling circle amplification strategy.•The assay exhibited a low detection limit of 0.001 U/mL for hOGG1.•The strategy showed excellent specificity over other nonspecific enzymes and good analytical performance in complex biological media.
ISSN:0956-5663
1873-4235
DOI:10.1016/j.bios.2015.12.106