JOURNAL OF SHANDONG UNIVERSITY(NATURAL SCIENCE) ›› 2016, Vol. 51 ›› Issue (3): 29-33.doi: 10.6040/j.issn.1671-9352.0.2015.456

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Fluorescence spectrometry study on the interaction between hydroxyl modified single-wall carbon nanotubes and bovine serum albumin/hemoglobin

LIU Yu-mei, WANG Hai-rong, LIU Shu-fang*   

  1. School of Public Health, Shandong University, Jinan 250012, Shandong, China
  • Received:2015-09-23 Online:2016-03-20 Published:2016-04-07

Abstract: The interaction between nanometer materials and biological macromolecules such as protein is an important content of biological safety of nano materials. This experiment aimed to study the interaction between hydroxyl modified single-wall carbon nanotubes and bovine serum albumin/hemoglobin. Two hydroxyl modified single-walled carbon nanotubes with different lengths(Short-SWNTs-OH and Long-SWNTs-OH)were chosen. The interaction between hydroxyl modified single-wall carbon nanotubes and bovine serum albumin/hemoglobin were investigated by fluorescence spectroscopy and synchronous fluorescence spectrometry under physiological conditions. The fluorescence spectra showed the intrinsic fluorescence of bovine serum albumin/hemoglobin could be quenched by two hydroxyl modified single-wall carbon nanotubes with concentration-effect relationship. For bovine serum albumin, the fluorescence quenching effect of Short-SWNTs-OH was more than that of Long-SWNTs-OH, while less different quenching effect of two carbon nanotubes was observed for bovine hemoglobin. The synchronous fluorescence spectra showed that the fluorescence quenching effect caused by Short-SWNTs-OH on tryptophan(Trp)residues was stronger than that of tyrosine(Tyr)residues. The above experimental results indicate that the carbon nanotubes morphology and protein type could 山 东 大 学 学 报 (理 学 版)第51卷 - 第3期刘玉梅,等:荧光光谱法研究羟基化单壁碳纳米管与牛血清白蛋白/血红蛋白的相互作用 \=-influence the interaction between them: hydroxyl single-walled carbon nanotubes combine more easily with bovine serum albumin compared to bovine hemoglobin, the length of hydroxyl single-walled carbon nanotubes and the types of protein could influence the interaction between carbon nanotubes and protein and the binding site of two carbon nanotubes to bovine serum albumin was located near tryptophan(Trp)residues. This study may provide reference for the biological safety evaluation of nanomaterials including carbon nanotubes.

Key words: carbon nanotubes, bovine serum albumin, bovine hemoglobin, fluorescence spectroscopy

CLC Number: 

  • O657.3
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