Issue 1, 2004

Protein immobilization on carbon nanotubesvia a two-step process of diimide-activated amidation

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

Article information

Article type
Communication
Submitted
27 Aug 2003
Accepted
28 Oct 2003
First published
06 Nov 2003

J. Mater. Chem., 2004,14, 37-39

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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