Journal
LANGMUIR
Volume 37, Issue 3, Pages 1001-1011Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.0c02095
Keywords
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Funding
- Labex ARCANE [ANR-11-LABX-0003-01]
- Graduate School on Chemistry, Biology and Health of Univ Grenoble Alpes CBH-EUR-GS [ANR-17-EURE-0003]
- Ministere de l'Environnement, de l'Energie et de la Mer
- Centre of Excellence of Multifunctional Architectured Material CEMAM - Investments for the Future Program [AN-10-LABX-44-01]
- ANR Multiplet [ANR-15-CE07-0021-01]
- platform Chimie NanoBio [ICMG FR 2607]
- Agence Nationale de la Recherche (ANR) [ANR-15-CE07-0021] Funding Source: Agence Nationale de la Recherche (ANR)
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Carbon nanotube electrodes were modified with ferrocene and laccase using click reactions strategies involving diazonium functionalization and oxime ligation, achieving a high surface coverage of ferrocene. The immobilization of active multicopper enzymes, laccases, on surfaces via copper(I)-catalyzed azide-alcyne cycloaddition was also successful, highlighting the efficiency of oxime-ligated dendrimers or cyclopeptides. Despite controlled orientation, this immobilization strategy was found to impact electron tunneling with enzyme active sites.
Carbon nanotube electrodes were modified with ferrocene and laccase using two different click reactions strategies and taking advantage of bifunctional dendrimers and cyclopeptides. Using diazonium functionalization and the efficiency of oxime ligation, the combination of both multiwalled carbon nanotube surfaces and modified dendrimers or cyclopeptides allows the access to a high surface coverage of ferrocene in the order of 50 nmol cm(-2), a 50-fold increase compared to a classic click reaction without oxime ligation of these highly branched macromolecules. Furthermore, this original immobilization strategy allows the immobilization of mono- and bi-functionalized active multicopper enzymes, laccases, via copper(I)-catalyzed azide-allcyne cycloaddition. Electrochemical studies underline the high efficiency of the oxime-ligated dendrimers or cyclopeptides for the immobilization of redox entities on surfaces while being detrimental to electron tunneling with enzyme active sites despite controlled orientation.
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