Amyloid-β detection with saccharide immobilized gold nanoparticle on carbon electrode

被引:114
作者
Chikae, Miyuki [2 ]
Fukuda, Tomohiro [2 ]
Kerman, Kagan [2 ]
Idegami, Koutarou [3 ]
Miura, Yoshiko [2 ]
Tamiya, Eiichi [1 ]
机构
[1] Osaka Univ, Grad Sch Engn, Dept Appl Phys, Suita, Osaka 5650871, Japan
[2] Japan Adv Inst Sci & Technol, Sch Mat Sci, Nomi City, Ishikawa 9231292, Japan
[3] Ishikawa Sunrise Ind CreationOrg, Kanazawa, Ishikawa 9208203, Japan
关键词
Sialic acid; Biosensor; Alzheimer's amyloid-beta peptide; Gold nanoparticle; Self-assembled monolayer; Voltammetry;
D O I
10.1016/j.bioelechem.2008.06.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The electrochemical sensing of saccharide-protein interactions using a couple of sialic acid derivatives and Alzheimer's amyloid-beta (A beta) is described. The densely-packed saccharide area for recognition of protein was fabricated onto a carbon electrode by three steps, which were electrochemical deposition of Au nanoparticles on a screen printed strip, self-assembled monolayer (SAM) formation of the acetylenyl group on Au nanoparticles, and the cycloaddition reaction of an azide-terminated sialic acid to the acetylenyl group. The attachment of A beta peptides to the sialic acid layer was confirmed by electrochemistry and atomic force microscopy imaging. The intrinsic oxidation signal of the captured A beta(1-40) and (1-42) peptides, containing a single tyrosine (Tyr) residues, was monitored at a peak potential of 0.6 V (vs Ag/AgCl within this sensor) in connection with differential pulse voltammetry. The peak current intensities were concentration dependent. The proposed process provides new routes for analysis of saccharide-protein interactions and electrochemical biosensor development. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:118 / 123
页数:6
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