Supramolecular cocaine-aptamer complexes activate biocatalytic cascades.
The anti-cocaine aptamer was fragmented into two nucleic acids, (1) and (2). The nucleic acid (1) was tethered at its 5'-end to aminoethyl nicotinamide adenine dinucleotide, amino-NAD(+), or to horseradish peroxidase, HRP. The nucleic acid (2) was functionalized at its 3'-end with alcohol dehydrogenase, AlcDH, or with glucose oxidase, GOx. In the presence of cocaine, the supramolecular NAD(+)/AlcDH/cocaine-aptamer complex is formed, and the biocatalytic oxidation of ethanol is activated. Similarly, in the presence of cocaine, the GOx/HRP/cocaine-aptamer complex is formed, and this activates the biocatalytic cascade where glucose is oxidized by GOx to yield gluconic acid and H(2)O(2), and the resulting hydrogen peroxide activates the HRP-biocatalyzed oxidation of 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonate), ABTS(2-). The systems may be considered as biomimetic prototypes for systems biology.
Freeman
Ronit
R
Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.
Sharon
Etery
E
Tel-Vered
Ran
R
Willner
Itamar
I
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D052157:Aptamers, Nucleotide / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D015374:Biosensing Techniques / Q000379:methods*; D003042:Cocaine / Q000032:analysis* / Q000378:metabolism; D000431:Ethanol / Q000378:metabolism; D005942:Gluconates / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D005949:Glucose Oxidase / Q000737:chemistry / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D009243:NAD / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction
D052157:Aptamers, Nucleotide; D005942:Gluconates; D009243:NAD; D000431:Ethanol; D006861:Hydrogen Peroxide; D000426:Alcohol Dehydrogenase; D005949:Glucose Oxidase; D006735:Horseradish Peroxidase; D003042:Cocaine; D005947:Glucose; C030691:gluconic acid