Direct, rapid, and label-free detection of enzyme-substrate interactions in physiological buffers using CMOS-compatible nanoribbon sensors

Nano Letters

Volumn 14, Issue 9, 2014, Pages 5315-5322

  Mu, Luye ^a   Droujinine, Ilia A ^b   Rajan, Nitin K ^a   Sawtelle, Sonya D ^a   Reed, Mark A ^a  

^a Yale University   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

enzyme activity detection; enzyme kinetics; enzyme substrate interaction; Nanobiosensors; pH sensing

Indexed keywords

ENZYME ACTIVITY; ENZYME KINETICS; NANORIBBONS; NANOWIRES; REACTION KINETICS; UREA;

ACETYLCHOLINESTERASE; ACTIVITY DETECTION; ENZYME-SUBSTRATE INTERACTIONS; MICHAELIS-MENTEN CONSTANT; NANO-BIOSENSORS; PH SENSING; PHOSPHATE-BUFFERED SALINES; PHYSIOLOGICAL BUFFERS;

ENZYME SENSORS;

ACETYLCHOLINE; ACETYLCHOLINESTERASE; ALUMINUM OXIDE; BUFFER; CARBON NANOTUBE; NANOWIRE; PENICILLIN DERIVATIVE; PENICILLINASE; PROTEIN BINDING; SILICON;

CHEMISTRY; COMPUTER PROGRAM; ENZYME SPECIFICITY; HYDROLYSIS; KINETICS; LIMIT OF DETECTION; NANOTECHNOLOGY; PH; PROCEDURES;

ACETYLCHOLINE; ACETYLCHOLINESTERASE; ALUMINUM OXIDE; BUFFERS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; LIMIT OF DETECTION; NANOTECHNOLOGY; NANOTUBES, CARBON; NANOWIRES; PENICILLINASE; PENICILLINS; PROTEIN BINDING; SILICON; SOFTWARE; SUBSTRATE SPECIFICITY;

EID: 84914132426     PISSN: 15306984     EISSN: 15306992     Source Type: Journal    
DOI: 10.1021/nl502366e     Document Type: Article

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