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001     17994
005     20240619090959.0
024 7 _ |2 pmid
|a pmid:22040747
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|a 10.1016/j.bios.2011.10.010
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041 _ _ |a eng
082 _ _ |a 570
100 1 _ |0 P:(DE-Juel1)VDB88034
|a Kisner, A.
|b 0
|u FZJ
245 _ _ |a Sensing small neurotransmitter enzyme interaction with nanoporous gated ion-sensitive field effect transistors
260 _ _ |a Amsterdam [u.a.]
|b Elsevier Science
|c 2012
300 _ _ |a 157–163
336 7 _ |a Journal Article
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336 7 _ |a article
|2 DRIVER
440 _ 0 |0 24721
|a Biosensors & Bioelectronics
|v 31
|y 157-163
500 _ _ |3 POF3_Assignment on 2016-02-29
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Ion-sensitive field effect transistors with gates having a high density of nanopores were fabricated and employed to sense the neurotransmitter dopamine with high selectivity and detectability at micromolar range. The nanoporous structure of the gates was produced by applying a relatively simple anodizing process, which yielded a porous alumina layer with pores exhibiting a mean diameter ranging from 20 to 35 nm. Gate-source voltages of the transistors demonstrated a pH-dependence that was linear over a wide range and could be understood as changes in surface charges during protonation and deprotonation. The large surface area provided by the pores allowed the physical immobilization of tyrosinase, which is an enzyme that oxidizes dopamine, on the gates of the transistors, and thus, changes the acid-base behavior on their surfaces. Concentration-dependent dopamine interacting with immobilized tyrosinase showed a linear dependence into a physiological range of interest for dopamine concentration in the changes of gate-source voltages. In comparison with previous approaches, a response time relatively fast for detecting dopamine was obtained. Additionally, selectivity assays for other neurotransmitters that are abundantly found in the brain were examined. These results demonstrate that the nanoporous structure of ion-sensitive field effect transistors can easily be used to immobilize specific enzyme that can readily and selectively detect small neurotransmitter molecule based on its acid-base interaction with the receptor. Therefore, it could serve as a technology platform for molecular studies of neurotransmitter-enzyme binding and drugs screening.
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588 _ _ |a Dataset connected to Pubmed
650 _ 2 |2 MeSH
|a Biosensing Techniques: instrumentation
650 _ 2 |2 MeSH
|a Conductometry: instrumentation
650 _ 2 |2 MeSH
|a Electrodes
650 _ 2 |2 MeSH
|a Enzymes, Immobilized: chemistry
650 _ 2 |2 MeSH
|a Equipment Design
650 _ 2 |2 MeSH
|a Equipment Failure Analysis
650 _ 2 |2 MeSH
|a Ions
650 _ 2 |2 MeSH
|a Monophenol Monooxygenase: chemistry
650 _ 2 |2 MeSH
|a Nanostructures: chemistry
650 _ 2 |2 MeSH
|a Nanostructures: ultrastructure
650 _ 2 |2 MeSH
|a Nanotechnology: instrumentation
650 _ 2 |2 MeSH
|a Neurotransmitter Agents: chemistry
650 _ 2 |2 MeSH
|a Porosity
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Interaction Mapping: instrumentation
650 _ 2 |2 MeSH
|a Reproducibility of Results
650 _ 2 |2 MeSH
|a Sensitivity and Specificity
650 _ 2 |2 MeSH
|a Transistors, Electronic
650 _ 7 |0 0
|2 NLM Chemicals
|a Enzymes, Immobilized
650 _ 7 |0 0
|2 NLM Chemicals
|a Ions
650 _ 7 |0 0
|2 NLM Chemicals
|a Neurotransmitter Agents
650 _ 7 |0 EC 1.14.18.1
|2 NLM Chemicals
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700 1 _ |0 P:(DE-Juel1)VDB26525
|a Stockmann, R.
|b 1
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700 1 _ |0 P:(DE-Juel1)VDB75326
|a Jansen, M.
|b 2
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700 1 _ |0 P:(DE-Juel1)VDB75222
|a Yegin, U.
|b 3
|u FZJ
700 1 _ |0 P:(DE-Juel1)128713
|a Offenhäusser, A.
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|u FZJ
700 1 _ |0 P:(DE-HGF)0
|a Kubota, L. T.
|b 5
700 1 _ |0 P:(DE-Juel1)VDB5576
|a Mourzina, Y.
|b 6
|u FZJ
773 _ _ |0 PERI:(DE-600)1496379-6
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|g Vol. 31
|n 1
|p 157–163
|q 31
|t Biosensors and bioelectronics
|v 31
|x 0956-5663
|y 2012
856 7 _ |u http://dx.doi.org/10.1016/j.bios.2011.10.010
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