Selective and direct immobilization of cysteinyl biomolecules by electrochemical cleavage of azo linkage

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 bi...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 26(2010), 19 vom: 05. Okt., Seite 15087-91
1. Verfasser: Jung, Hyun Joo (VerfasserIn)
Weitere Verfasser: Hwang, Inseong, Kim, Beom Jin, Min, Hyegeun, Yu, Hyunung, Lee, Tae Geol, Chung, Taek Dong
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2010
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Azo Compounds Peptides Cysteine K848JZ4886
Beschreibung
Zusammenfassung: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
Beschreibung:Date Completed 03.01.2011
Date Revised 21.11.2013
published: Print
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/la102489k