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Updated: Jul 10, 2026

Engineering Molecular Recognition with Bio-mimetic Polymers on Single Walled Carbon Nanotubes
Published on: January 10, 2017
Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes
Prashanth Asuri1, Shyam Sundhar Bale, Ravindra C Pangule
1Department of Chemical and Biological Engineering, Center for Biotechnology & Interdisciplinary Studies, Rensselaer Nanotechnology Center, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Abstract:
We describe the structure, activity, and stability of enzymes covalently attached to single-walled carbon nanotubes (SWNTs). Conjugates of SWNTs with three functionally unrelated enzymes-horseradish peroxidase, subtilisin Carlsberg, and chicken egg white lysozyme-were found to be soluble in aqueous solutions. Furthermore, characterization of the secondary and tertiary structure of the immobilized proteins by circular dichroism and fluorescence spectroscopies, respectively, and determination of enzyme kinetics revealed that the enzymes retained a high fraction of their native structure and activity upon attachment to SWNTs. The SWNT-enzyme conjugates were also more stable in guanidine hydrochloride (GdnHCl) and at elevated temperatures relative to their solution counterparts. Thus, these protein conjugates represent novel preparations that possess the attributes of both soluble enzymes-high activity and low diffusional resistance-and immobilized enzymes-high stability-making them attractive choices for applications ranging from diagnostics and sensing to drug delivery.
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