Design of Maleimide: Functionalised Electrodes for Covalent Attachment of Proteins through Free Surface Cysteine Groups

Emma J. Wright, Maciej Sosna, Sally Bloodworth*, Jeremy D. Kilburn, Philip N. Bartlett

*Corresponding author for this work

    Research output: Contribution to journalArticle

    7 Citations (Scopus)

    Abstract

    Mixed two-component monolayers on glassy carbon are prepared by electrochemical oxidation of N-(2-aminoethyl)acetamide and mono-N-Boc-hexamethylenediamine in mixed solution. Subsequent N-deprotection, amide coupling and solid-phase synthetic steps lead to electrode-surface functionalisation with maleimide, with controlled partial coverage of this cysteine-binding group at appropriate dilution for covalent immobilisation of a model redox-active protein, cytochrome c, with high coverage (approximate to 7.5pmolcm(-2)).

    Original languageEnglish
    Pages (from-to)5550-5554
    Number of pages5
    JournalChemistry : a European Journal
    Volume20
    Issue number19
    Early online date2 May 2014
    DOIs
    Publication statusPublished - 5 May 2014

    Cite this

    Design of Maleimide : Functionalised Electrodes for Covalent Attachment of Proteins through Free Surface Cysteine Groups. / Wright, Emma J.; Sosna, Maciej; Bloodworth, Sally; Kilburn, Jeremy D.; Bartlett, Philip N.

    In: Chemistry : a European Journal, Vol. 20, No. 19, 05.05.2014, p. 5550-5554.

    Research output: Contribution to journalArticle

    Wright, Emma J. ; Sosna, Maciej ; Bloodworth, Sally ; Kilburn, Jeremy D. ; Bartlett, Philip N. / Design of Maleimide : Functionalised Electrodes for Covalent Attachment of Proteins through Free Surface Cysteine Groups. In: Chemistry : a European Journal. 2014 ; Vol. 20, No. 19. pp. 5550-5554.
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    abstract = "Mixed two-component monolayers on glassy carbon are prepared by electrochemical oxidation of N-(2-aminoethyl)acetamide and mono-N-Boc-hexamethylenediamine in mixed solution. Subsequent N-deprotection, amide coupling and solid-phase synthetic steps lead to electrode-surface functionalisation with maleimide, with controlled partial coverage of this cysteine-binding group at appropriate dilution for covalent immobilisation of a model redox-active protein, cytochrome c, with high coverage (approximate to 7.5pmolcm(-2)).",
    author = "Wright, {Emma J.} and Maciej Sosna and Sally Bloodworth and Kilburn, {Jeremy D.} and Bartlett, {Philip N.}",
    note = "Acknowledgements We thank H. Hamzah for running background voltammograms on the unmodified glassy carbon electrodes. This work was funded by the European Research Council, project 3D-Nano-BioDevice NMP4-SL-2009–22925.",
    year = "2014",
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    doi = "10.1002/chem.201400246",
    language = "English",
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    TY - JOUR

    T1 - Design of Maleimide

    T2 - Functionalised Electrodes for Covalent Attachment of Proteins through Free Surface Cysteine Groups

    AU - Wright, Emma J.

    AU - Sosna, Maciej

    AU - Bloodworth, Sally

    AU - Kilburn, Jeremy D.

    AU - Bartlett, Philip N.

    N1 - Acknowledgements We thank H. Hamzah for running background voltammograms on the unmodified glassy carbon electrodes. This work was funded by the European Research Council, project 3D-Nano-BioDevice NMP4-SL-2009–22925.

    PY - 2014/5/5

    Y1 - 2014/5/5

    N2 - Mixed two-component monolayers on glassy carbon are prepared by electrochemical oxidation of N-(2-aminoethyl)acetamide and mono-N-Boc-hexamethylenediamine in mixed solution. Subsequent N-deprotection, amide coupling and solid-phase synthetic steps lead to electrode-surface functionalisation with maleimide, with controlled partial coverage of this cysteine-binding group at appropriate dilution for covalent immobilisation of a model redox-active protein, cytochrome c, with high coverage (approximate to 7.5pmolcm(-2)).

    AB - Mixed two-component monolayers on glassy carbon are prepared by electrochemical oxidation of N-(2-aminoethyl)acetamide and mono-N-Boc-hexamethylenediamine in mixed solution. Subsequent N-deprotection, amide coupling and solid-phase synthetic steps lead to electrode-surface functionalisation with maleimide, with controlled partial coverage of this cysteine-binding group at appropriate dilution for covalent immobilisation of a model redox-active protein, cytochrome c, with high coverage (approximate to 7.5pmolcm(-2)).

    U2 - 10.1002/chem.201400246

    DO - 10.1002/chem.201400246

    M3 - Article

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    JO - Chemistry : a European Journal

    JF - Chemistry : a European Journal

    SN - 0947-6539

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    ER -