Electrochemical cleavage of azo linkage for site-selective immobilization and cell patterning.
A new molecular structure of azobenzene, which can be reduced to the corresponding anilines at a low reduction potential for the site-selective immobilization of biomolecules, is proposed. Redox-active species, enzymes, peptides, and cultured hippocampal neurons can be effectively immobilized on the electrochemically activated surface.
Jung
Hyun Joo
HJ
Department of Chemistry, Seoul National University, Seoul 151-747, Korea.
Min
Hyegeun
H
Yu
Hyunung
H
Lee
Tae Geol
TG
Chung
Taek Dong
TD
D000595:Amino Acid Sequence; D000818:Animals; D001391:Azo Compounds / Q000737:chemistry*; D055664:Electrochemical Techniques; D055767:Immobilized Proteins / Q000737:chemistry; D009474:Neurons / Q000166:cytology; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry; D013499:Surface Properties
D001391:Azo Compounds; D055767:Immobilized Proteins; D010455:Peptides; C009850:azobenzene