Nanostructured biosensor for measuring neuropathy target esterase activity

Neeraj Kohli, Devesh Srivastava, Jun Sun, Rudy J. Richardson, Ilsoon Lee, Robert M. Worden

    Research output: Contribution to journalArticle

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    Abstract

    Neuropathy target esterase (NTE) is a membrane protein found in human neurons and other cells, including lymphocytes. Binding of certain organophosphorus (OP) compounds to NTE is believed to cause OP-induced delayed neuropathy (OPIDN), a type of paralysis for which there is no effective treatment. Mutations in NTE have also been linked with serious neurological diseases, such as motor neuron disease. This paper describes development of the first nanostructured biosensor interface containing a catalytically active fragment of NTE known as NEST. The biosensor was fabricated using the layer-by-layer assembly approach, by immobilizing a layer of NEST on top of multilayers consisting of a polyelectrolyte (poly-L-lysine) and an enzyme (tyrosinase). The biosensor has a response time on the order of seconds and gives a concentration-dependent decrease in sensor output in response to a known NEST (and NTE) inhibitor. Potential applications of the biosensor include screening OP compounds for NTE inhibition and investigating the enzymology of wild-type and mutant forms of NTE. Although the development of a NEST biosensor was the primary purpose of this study, we found that the approach developed for NEST could also be extended to measure the activity of other esterases involved in neural processes, such as acetyl-cholinesterase (AChE) and butyrylcholinesterase (BChE). On the basis of measured sensitivities, phenyl valerate was the preferred substrate for NEST and BChE, whereas phenyl acetate was better for AChE.

    Original languageEnglish (US)
    Pages (from-to)5196-5203
    Number of pages8
    JournalAnalytical Chemistry
    Volume79
    Issue number14
    DOIs
    StatePublished - Jul 15 2007

    Profile

    Biosensors
    Supravalvular Aortic Stenosis
    Nitrogenase
    Artificial Organs
    Magnesium Deficiency
    Tetany
    Dental Materials
    Micelles
    Substrates

    ASJC Scopus subject areas

    • Analytical Chemistry

    Cite this

    Nanostructured biosensor for measuring neuropathy target esterase activity. / Kohli, Neeraj; Srivastava, Devesh; Sun, Jun; Richardson, Rudy J.; Lee, Ilsoon; Worden, Robert M.

    In: Analytical Chemistry, Vol. 79, No. 14, 15.07.2007, p. 5196-5203.

    Research output: Contribution to journalArticle

    Kohli, N, Srivastava, D, Sun, J, Richardson, RJ, Lee, I & Worden, RM 2007, 'Nanostructured biosensor for measuring neuropathy target esterase activity' Analytical Chemistry, vol 79, no. 14, pp. 5196-5203. DOI: 10.1021/ac0701684
    Kohli N, Srivastava D, Sun J, Richardson RJ, Lee I, Worden RM. Nanostructured biosensor for measuring neuropathy target esterase activity. Analytical Chemistry. 2007 Jul 15;79(14):5196-5203. Available from, DOI: 10.1021/ac0701684

    Kohli, Neeraj; Srivastava, Devesh; Sun, Jun; Richardson, Rudy J.; Lee, Ilsoon; Worden, Robert M. / Nanostructured biosensor for measuring neuropathy target esterase activity.

    In: Analytical Chemistry, Vol. 79, No. 14, 15.07.2007, p. 5196-5203.

    Research output: Contribution to journalArticle

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    abstract = "Neuropathy target esterase (NTE) is a membrane protein found in human neurons and other cells, including lymphocytes. Binding of certain organophosphorus (OP) compounds to NTE is believed to cause OP-induced delayed neuropathy (OPIDN), a type of paralysis for which there is no effective treatment. Mutations in NTE have also been linked with serious neurological diseases, such as motor neuron disease. This paper describes development of the first nanostructured biosensor interface containing a catalytically active fragment of NTE known as NEST. The biosensor was fabricated using the layer-by-layer assembly approach, by immobilizing a layer of NEST on top of multilayers consisting of a polyelectrolyte (poly-L-lysine) and an enzyme (tyrosinase). The biosensor has a response time on the order of seconds and gives a concentration-dependent decrease in sensor output in response to a known NEST (and NTE) inhibitor. Potential applications of the biosensor include screening OP compounds for NTE inhibition and investigating the enzymology of wild-type and mutant forms of NTE. Although the development of a NEST biosensor was the primary purpose of this study, we found that the approach developed for NEST could also be extended to measure the activity of other esterases involved in neural processes, such as acetyl-cholinesterase (AChE) and butyrylcholinesterase (BChE). On the basis of measured sensitivities, phenyl valerate was the preferred substrate for NEST and BChE, whereas phenyl acetate was better for AChE.",
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