Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications

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Standard

Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications. / Risveden, Klas; Dick, Kimberly A; Bhand, Sunil; Rydberg, Patrik Åke Anders; Samuelson, Lars; Danielsson, Bengt.

I: Nanotechnology, Bind 21, Nr. 5, 2010, s. 055102.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Risveden, K, Dick, KA, Bhand, S, Rydberg, PÅA, Samuelson, L & Danielsson, B 2010, 'Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications', Nanotechnology, bind 21, nr. 5, s. 055102. https://doi.org/10.1088/0957-4484/21/5/055102

APA

Risveden, K., Dick, K. A., Bhand, S., Rydberg, P. Å. A., Samuelson, L., & Danielsson, B. (2010). Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications. Nanotechnology, 21(5), 055102. https://doi.org/10.1088/0957-4484/21/5/055102

Vancouver

Risveden K, Dick KA, Bhand S, Rydberg PÅA, Samuelson L, Danielsson B. Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications. Nanotechnology. 2010;21(5):055102. https://doi.org/10.1088/0957-4484/21/5/055102

Author

Risveden, Klas ; Dick, Kimberly A ; Bhand, Sunil ; Rydberg, Patrik Åke Anders ; Samuelson, Lars ; Danielsson, Bengt. / Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications. I: Nanotechnology. 2010 ; Bind 21, Nr. 5. s. 055102.

Bibtex

@article{09a402201a3011df8ed1000ea68e967b,
title = "Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications",
abstract = "A novel lab-on-a-chip nanotree enzyme reactor is demonstrated for the detection of acetylcholine. The reactors are intended for use in the RISFET (regional ion sensitive field effect transistor) nanosensor, and are constructed from gold-tipped branched nanorod structures grown on SiN(x)-covered wafers. Two different reactors are shown: one with simple, one-dimensional nanorods and one with branched nanorod structures (nanotrees). Significantly higher enzymatic activity is found for the nanotree reactors than for the nanorod reactors, most likely due to the increased gold surface area and thereby higher enzyme binding capacity. A theoretical calculation is included to show how the enzyme kinetics and hence the sensitivity can be influenced and increased by the control of electrical fields in relation to the active sites of enzymes in an electronic biosensor. The possible effects of electrical fields employed in the RISFET on the function of acetylcholine esterase is investigated using quantum chemical methods, which show that the small electric field strengths used are unlikely to affect enzyme kinetics. Acetylcholine esterase activity is determined using choline oxidase and peroxidase by measuring the amount of choline formed using the chemiluminescent luminol reaction.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Klas Risveden and Dick, {Kimberly A} and Sunil Bhand and Rydberg, {Patrik {\AA}ke Anders} and Lars Samuelson and Bengt Danielsson",
year = "2010",
doi = "10.1088/0957-4484/21/5/055102",
language = "English",
volume = "21",
pages = "055102",
journal = "Nanotechnology",
issn = "0957-4484",
publisher = "Institute of Physics Publishing Ltd",
number = "5",

}

RIS

TY - JOUR

T1 - Branched nanotrees with immobilized acetylcholine esterase for nanobiosensor applications

AU - Risveden, Klas

AU - Dick, Kimberly A

AU - Bhand, Sunil

AU - Rydberg, Patrik Åke Anders

AU - Samuelson, Lars

AU - Danielsson, Bengt

PY - 2010

Y1 - 2010

N2 - A novel lab-on-a-chip nanotree enzyme reactor is demonstrated for the detection of acetylcholine. The reactors are intended for use in the RISFET (regional ion sensitive field effect transistor) nanosensor, and are constructed from gold-tipped branched nanorod structures grown on SiN(x)-covered wafers. Two different reactors are shown: one with simple, one-dimensional nanorods and one with branched nanorod structures (nanotrees). Significantly higher enzymatic activity is found for the nanotree reactors than for the nanorod reactors, most likely due to the increased gold surface area and thereby higher enzyme binding capacity. A theoretical calculation is included to show how the enzyme kinetics and hence the sensitivity can be influenced and increased by the control of electrical fields in relation to the active sites of enzymes in an electronic biosensor. The possible effects of electrical fields employed in the RISFET on the function of acetylcholine esterase is investigated using quantum chemical methods, which show that the small electric field strengths used are unlikely to affect enzyme kinetics. Acetylcholine esterase activity is determined using choline oxidase and peroxidase by measuring the amount of choline formed using the chemiluminescent luminol reaction.

AB - A novel lab-on-a-chip nanotree enzyme reactor is demonstrated for the detection of acetylcholine. The reactors are intended for use in the RISFET (regional ion sensitive field effect transistor) nanosensor, and are constructed from gold-tipped branched nanorod structures grown on SiN(x)-covered wafers. Two different reactors are shown: one with simple, one-dimensional nanorods and one with branched nanorod structures (nanotrees). Significantly higher enzymatic activity is found for the nanotree reactors than for the nanorod reactors, most likely due to the increased gold surface area and thereby higher enzyme binding capacity. A theoretical calculation is included to show how the enzyme kinetics and hence the sensitivity can be influenced and increased by the control of electrical fields in relation to the active sites of enzymes in an electronic biosensor. The possible effects of electrical fields employed in the RISFET on the function of acetylcholine esterase is investigated using quantum chemical methods, which show that the small electric field strengths used are unlikely to affect enzyme kinetics. Acetylcholine esterase activity is determined using choline oxidase and peroxidase by measuring the amount of choline formed using the chemiluminescent luminol reaction.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1088/0957-4484/21/5/055102

DO - 10.1088/0957-4484/21/5/055102

M3 - Journal article

C2 - 20023308

VL - 21

SP - 055102

JO - Nanotechnology

JF - Nanotechnology

SN - 0957-4484

IS - 5

ER -

ID: 17655148