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Anal Bioanal Chem ; 401(10): 3229-34, 2011 Dec.
Article in English | MEDLINE | ID: mdl-21975602

ABSTRACT

A novel fluorescence polarization (FP) aptasensing platform based on target-induced aptamer enzymatic cleavage protection is reported. The method relies on the FP analysis of the phosphodiesterase I mediated size variation of a dye-labeled aptamer. The tyrosinamide/antityrosinamide DNA aptamer couple was firstly tested as a model system to establish the proof-of-concept. In the absence of the target, the labeled aptamer was enzymatically cleaved into small DNA fragments, leading to a low FP signal. Upon tyrosinamide binding, the DNA substrate was partially protected against the enzymatic attack, leading to an increase in the fluorescence anisotropy response as a result of the higher average molecular volume of the weakly digested probe. The method was subsequently applied to two other systems, i.e., for the detection of ochratoxin A and adenosine. Such an approach was found to combine simplicity and general applicability features.


Subject(s)
Aptamers, Nucleotide/chemistry , Biosensing Techniques/methods , Fluorescence Polarization/methods , Phosphodiesterase I/chemistry , Adenosine/analysis , Biosensing Techniques/instrumentation , Fluorescence Polarization/instrumentation , Fluorescent Dyes/chemistry , Ochratoxins/analysis
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