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

Kuiyang Jiang, Linda S. Schadler, Richard W. Siegel, Xinjie Zhang, Haifeng Zhang, Mauricio Terrones

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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 CN x 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.

Original languageEnglish (US)
Pages (from-to)37-39
Number of pages3
JournalJournal of Materials Chemistry
Volume14
Issue number1
DOIs
StatePublished - Jan 7 2004

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All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Materials Chemistry

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