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Issue 1, 2004
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Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation

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Abstract

Ferritin and bovine serum albumin (BSA) proteins are chemically bonded to nitrogen-doped multi-walled carbon nanotubes (CNx MWNTs) through a two-step process of diimide-activated amidation. First, carboxylated CNx MWNTs were activated by N-ethyl-N′-(3-dimethylaminopropyl)carbodiimide hydrochloride (EDAC), forming a stable active ester in the presence of N-hydroxysuccinimide (NHS). Second, the active ester was reacted with the amine groups on the proteins of ferritin or BSA, forming an amide bond between the CNx MWNTs and proteins. This two-step process avoids the intermolecular conjugation of proteins, and guarantees the uniform attachment of proteins on carbon nanotubes. TEM and AFM measurements clearly confirmed the successful attachment. This approach provides a universal and efficient method to attach biomolecules to carbon nanotubes at ambient conditions.

Graphical abstract: Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation

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Publication details

The article was received on 27 Aug 2003, accepted on 28 Oct 2003 and first published on 06 Nov 2003


Article type: Communication
DOI: 10.1039/B310359E
Citation: J. Mater. Chem., 2004,14, 37-39
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    Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation

    K. Jiang, L. S. Schadler, R. W. Siegel, X. Zhang, H. Zhang and M. Terrones, J. Mater. Chem., 2004, 14, 37
    DOI: 10.1039/B310359E

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