Selective and Direct Immobilization of Cysteinyl Biomolecules by Electrochemical Cleavage of Azo Linkage

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• 作者：Hyun Joo Jung ; Inseong Hwang ; Beom Jin Kim ; Hyegeun Min ; Hyunung Yu ; Tae Geol Lee ; Taek Dong Chung
• 刊名：Langmuir
• 出版年：2010
• 出版时间：October 5, 2010
• 年：2010
• 卷：26
• 期：19
• 页码：15087-15091
• 全文大小：922K
• 年卷期：v.26,no.19(October 5, 2010)
• ISSN：1520-5827

文摘

Controlled orientation and reserved activity of biomolecules, when site-selectively immobilized in a highly integrated manner on a minimal time scale, are crucial in designing biosensors for the multiplex detection. Here, we describe a novel method for the orientation-controlled immobilization of biomolecules based on site-selective electrochemical activation of p-hydroxyazobenzene self-assembled monolayer (SAM) followed by one-step coupling of cysteinyl biomolecules. The p-aminophenol, a product of reductive cleavage of p-hydroxyazobenzene, was subsequently oxidized to yield p-quinoneimine which then conjugated with cysteinyl biomolecules through 1,4-Michael addition, thus obviating additional linker agents and the related time consumption. Using this method, we selectively activated the electrode surface and immobilized laminin peptide IKVAV, a neurite promoting motif. When we cultured hippocampal neurons on the electrode, the extended neurites were found only within the electrochemically activated area. Hence, the proposed method represents a new promising platform for the patterning of functional peptides, active proteins, and live cells.