Protein-affinity of single-walled carbon nanotubes in water

被引：143

作者：

Lin, Y

Allard, LF

Sun, YP ^{[1
]}

机构：

[1] Clemson Univ, Howard L Hunter Chem Lab, Dept Chem, Clemson, SC 29634 USA

[2] Oak Ridge Natl Lab, High Temp Mat Lab, Oak Ridge, TN 37831 USA

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2004年 / 108卷 / 12期

关键词：

D O I：

10.1021/jp031248o

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The interactions of single-walled carbon nanotubes (SWNTs) with ferritin protein in water were investigated. It was found that SWNTs are naturally protein-affinitive in an aqueous ferritin solution, resulting in significant ferritin-SWNT conjugation and the solubilization of the nanotubes. The conjugation is further enhanced and stabilized in the presence of a coupling agent for amidation to promote the formation of covalent linkages. The natural protein-affinity of SWNTs may be alleviated or even eliminated by the functionalization of the nanotubes with hydrophilic polymers or better with oligomeric poly(ethylene glycol) moieties.

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页码：3760 / 3764

页数：5

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