Immobilization of aptamer-modified gold nanoparticles on BiOCl nanosheets: Tunable peroxidase-like activity by protein recognition

被引:55
作者
Hsu, Chia-Lun [1 ]
Lien, Chia-Wen [1 ]
Wang, Chia-Wei [1 ]
Harroun, Scott G. [1 ]
Huang, Chih-Ching [2 ,3 ,4 ]
Chang, Huan-Tsung [1 ]
机构
[1] Natl Taiwan Univ, Dept Chem, Taipei 10617, Taiwan
[2] Natl Taiwan Ocean Univ, Dept Biosci & Biotechnol, Keelung 20224, Taiwan
[3] Natl Taiwan Ocean Univ, Ctr Excellence Oceans, Keelung 20224, Taiwan
[4] Kaohsiung Med Univ, Coll Pharm, Sch Pharm, Kaohsiung 80708, Taiwan
关键词
Enzyme; Self-assembly; Nanoparticles; Aptamers; Synergistic effects; DISPERSED CARBON NANOTUBES; ENDOTHELIAL GROWTH-FACTOR; ENZYME-LIKE ACTIVITY; GRAPHENE OXIDE; CATALYTIC-ACTIVITY; 001; FACETS; NANOMATERIALS; IMPROVEMENT; OXIDATION; MIMICS;
D O I
10.1016/j.bios.2015.08.049
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
A self-assembled nanocomposite is prepared from an aqueous mixture of aptamer-modified gold nanoparticles (Apt-Au NPs), bismuth ions and chloride ions. The Apt-Au NPs are immobilized on bismuth oxychloride (BiOCl) nanosheets in situ to form Apt-Au NPs/BiOCl nanocomposites. The as-prepared nanocomposites exhibit high peroxidase-like activity for the catalytic conversion of Amplest Red (AR) to fluorescent resorufin in the presence of H2O2. The catalytic activity of Apt-Au NPs/BiOCl nanocomposites is at least 90-fold higher than that of Apt-Au NPs or BiOCl nanosheets, revealing synergistic effects on their activity. The catalytic activity of Apt-Au NPs/BiOCl nanocomposites is suppressed by vascular endothelial growth factor-A(165) (VEGF-A(165)) molecules that specifically interact with the aptamer units (Del-5-1 and v7t-1) on the nanocomposite surface. The AR/H2O2-Apt-Au NPs/BiOCl nanocomposites probe shows high selectivity (> 1000-fold over other proteins) and sensitivity (detection limit similar to 0.5 nM) for the detection of VEGF-A(165). Furthermore, the probe is employed for the detection of VEGF isoforms and for the study of interactions between VEGF and VEGF receptors. The practicality of this simple, rapid, cost-effective probe is validated by the analysis of VEGF-A(165) in cell culture media, showing its great potential for the analysis of VEGF in biological samples. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:181 / 187
页数:7
相关论文
共 47 条
[1]   Review of iron-free Fenton-like systems for activating H2O2 in advanced oxidation processes [J].
Bokare, Alok D. ;
Choi, Wonyong .
JOURNAL OF HAZARDOUS MATERIALS, 2014, 275 :121-135
[2]   Facile synthesis of BiOCl nano-flowers of narrow band gap and their visible-light-induced photocatalytic property [J].
Chen, Lang ;
Yin, Shuang-Feng ;
Huang, Rui ;
Zhou, Yan ;
Luo, Sheng-Lian ;
Au, Chak-Tong .
CATALYSIS COMMUNICATIONS, 2012, 23 :54-57
[3]   Peroxidase-Like Activity of Cupric Oxide Nanoparticle [J].
Chen, Wei ;
Chen, Juan ;
Liu, Ai-Lin ;
Wang, Li-Man ;
Li, Guang-Wen ;
Lin, Xin-Hua .
CHEMCATCHEM, 2011, 3 (07) :1151-1154
[4]   Dual Enzyme-like Activities of Iron Oxide Nanoparticles and Their Implication for Diminishing Cytotoxicity [J].
Chen, Zhongwen ;
Yin, Jun-Jie ;
Zhou, Yu-Ting ;
Zhang, Yu ;
Song, Lina ;
Song, Mengjie ;
Hu, Sunling ;
Gu, Ning .
ACS NANO, 2012, 6 (05) :4001-4012
[5]   Mesoporous material-based manipulation of the enzyme-like activity of CoFe2O4 nanoparticles [J].
Fan, Yingwei ;
Shi, Wenbing ;
Zhang, Xiaodan ;
Huang, Yuming .
JOURNAL OF MATERIALS CHEMISTRY A, 2014, 2 (08) :2482-2486
[6]   The biology of VEGF and its receptors [J].
Ferrara, N ;
Gerber, HP ;
LeCouter, J .
NATURE MEDICINE, 2003, 9 (06) :669-676
[7]   Discovery and Current Application of Nanozyme [J].
Gao Li-Zeng ;
Yan Xi-Yun .
PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS, 2013, 40 (10) :892-902
[8]   Explicit reformulations of time-dependent solution for a Michaelis-Menten enzyme reaction model [J].
Golicnik, Marko .
ANALYTICAL BIOCHEMISTRY, 2010, 406 (01) :94-96
[9]   3D hierarchically porous Cu-BiOCl nanocomposite films: one-step electrochemical synthesis, structural characterization and nanomechanical and photoluminescent properties [J].
Guerrero, Miguel ;
Pane, Salvador ;
Nelson, Bradley J. ;
Baro, Maria Dolors ;
Roldan, Onica ;
Sort, Jordi ;
Pellicer, Eva .
NANOSCALE, 2013, 5 (24) :12542-12550
[10]   Improvement of aptamer affinity by dimerization [J].
Hasegawa, Hijiri ;
Taira, Ken-ichi ;
Sode, Koji ;
Ikebukuro, Kazunori .
SENSORS, 2008, 8 (02) :1090-1098