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Study of Specific Binding of Maltose Binding Protein to Pyrrole-Derived Bipyridinium Film by Quartz Crystal Microbalance
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    Study of Specific Binding of Maltose Binding Protein to Pyrrole-Derived Bipyridinium Film by Quartz Crystal Microbalance
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    Department of Chemistry and Chemical Biology, Baker Laboratory, Department of Food Science, Stocking Hall, and Department of Microbiology, Wing Hall, Cornell University, Ithaca, New York 14853
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    Langmuir

    Cite this: Langmuir 2002, 18, 12, 4892–4897
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    https://doi.org/10.1021/la0116950
    Published May 15, 2002
    Copyright © 2002 American Chemical Society

    Abstract

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    The affinity of the maltose binding protein−nitro reductase fusion (MBP−NR) to electropolymerized films of N-(3-pyrrol-1-ylpropyl)-4,4‘-bipyridinium (PPB) has been studied in aqueous medium by the quartz crystal microbalance (QCM) technique. It was found that the MBP domain of MBP−NR exhibits specific binding toward PPB films through the maltose binding site and that the immobilized MBP−NR retains its enzymatic activity toward trinitrotoluene (TNT) reduction. Although some MBP−NR was nonspecifically adsorbed onto a maltose-covered PPB film as well as to a bare Au electrode, in both cases the adsorbed enzyme exhibited no catalytic activity. Nitro reductase (NR) also appeared to adsorb onto the PPB films but did not exhibit any enzymatic activity. The electropolymerization of N-(3-pyrrol-1-ylpropyl)-4,4‘-bipyridinium (PPB) onto a Au electrode in acetonitrile solution was studied by electrochemical quartz crystal microbalance (EQCM). It was found that the extent of polymerization upon pyrrole-centered oxidation decreased with continuous potential scanning. The bipyridinium-localized (quaternized nitrogen) redox reaction appeared to be of the anion-exchange type.

    Copyright © 2002 American Chemical Society

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     Department of Chemistry and Chemical Biology.

     Department of Food Science.

    §

     Department of Microbiology.

    *

    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

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    This article is cited by 6 publications.

    1. Kazutake Takada,, Zeki Naal, and, Héctor D. Abruña. Detailed Study of N-(3-Pyrrol-1-yl-propyl)-4,4‘-bipyridinium (PPB) Electropolymerization. Langmuir 2003, 19 (13) , 5402-5406. https://doi.org/10.1021/la020957a
    2. Zeki Naal, Rose Mary Zumstein Georgetto Naal. Quartz Crystal Microbalance in Bioanalysis. 2022, 313-330. https://doi.org/10.1007/978-3-030-82381-8_17
    3. Kyoungsook Park, Lan Hee Lee, Yong-Beom Shin, So Yeon Yi, Yong-Won Kang, Dai-Eun Sok, Jin Woong Chung, Bong Hyun Chung, Moonil Kim. Detection of conformationally changed MBP using intramolecular FRET. Biochemical and Biophysical Research Communications 2009, 388 (3) , 560-564. https://doi.org/10.1016/j.bbrc.2009.08.049
    4. Matthew A. Cooper, Victoria T. Singleton. A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: applications of acoustic physics to the analysis of biomolecular interactions. Journal of Molecular Recognition 2007, 20 (3) , 154-184. https://doi.org/10.1002/jmr.826
    5. Igor L Medintz, Jeffrey R Deschamps. Maltose-binding protein: a versatile platform for prototyping biosensing. Current Opinion in Biotechnology 2006, 17 (1) , 17-27. https://doi.org/10.1016/j.copbio.2006.01.002
    6. Guifeng Li, Shigeaki Morita, Shen Ye, Masaru Tanaka, Masatoshi Osawa. Quartz Crystal Microbalance and Infrared Reflection Absorption Spectroscopy Characterization of Bisphenol A Absorption in the Poly(acrylate) Thin Films. Analytical Chemistry 2004, 76 (3) , 788-795. https://doi.org/10.1021/ac0348874

    Langmuir

    Cite this: Langmuir 2002, 18, 12, 4892–4897
    Click to copy citationCitation copied!
    https://doi.org/10.1021/la0116950
    Published May 15, 2002
    Copyright © 2002 American Chemical Society

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