Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes

被引:145
作者
Asuri, Prashanth [1 ]
Bale, Shyam Sundhar [1 ]
Pangule, Ravindra C. [1 ]
Shah, Dhiral A. [1 ]
Kane, Ravi S. [1 ]
Dordick, Jonathan S. [1 ]
机构
[1] Rensselaer Polytech Inst, Rensselaer Nanotechnol Ctr, Ctr Biotechnol & Interdisciplinary Studies, Dept Biol & Chem Engn, Troy, NY 12180 USA
关键词
D O I
10.1021/la702091c
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:12318 / 12321
页数:4
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