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Versatile DNAzyme-based Amplified Biosensing Platforms for Nucleic Acid, Protein and Enzyme Activity Detection.
MedLine Citation:
PMID:  23406194     Owner:  NLM     Status:  Publisher    
DNAzymes have been widely applied as signal amplifiers for enzyme-free and highly sensitive detection of DNA. A few of them have also been employed for amplified detection of other biomolecules via a target-triggered assembly of split or mutated DNAzyme strategy. However, most of these designs adopt Mg2+-dependent DNAzyme as catalytic unit, which suffered from low catalytic cleavage activity. Meanwhile, some DNAzymes with high catalytic activity are not suitable for these designs because the slight modification of the catalytic core might results in remarkably decreased or even no catalytic activity of these DNAzymes. Based on DNAzyme topological effect or the terminal protection of small-molecule-linked DNA, we developed two versatile sensing platforms for amplified detection of different biotargets. Since no modification is necessary for the catalytic core of the DNAzyme in these designs, they can employ any DNAzyme with high catalytic activity as amplified unit, which affords a high amplified efficiency for the sensing platform. A catalytic and molecular beacon design was further employed to realize the true enzymatic multiple turnover of DNAzyme. These designs together allow a high sensitivity for the biotargets, resulting in a detection limit of 20 pM, 0.2 U/mL and 1 ng/mL for target DNA, DNA adenine methylation methyltransferase (Dam MTase) and streptavidin, respectively, much lower than previously reported biosensors. In addition, the proposed sensing strategy is versatile. By conjugating with various recognition units, it can be employed to detect a wide range of biotargets, varying from nucleic acids to proteins with high sensitivity.
Xuhua Zhao; Liang Gong; Xiaobing Zhang; Bin Yang; Ting Fu; Rong Hu; Weihong Tan; Ru-Qin Yu
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-2-14
Journal Detail:
Title:  Analytical chemistry     Volume:  -     ISSN:  1520-6882     ISO Abbreviation:  Anal. Chem.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-2-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370536     Medline TA:  Anal Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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