Thin film which consisted of metalloprotein via various chemical linker was fabricated to investigate linker-length effect between immobilized protein and Au surface. A metalloprotein was utilized the myoglobin which has redox property due to the iron ions of heme group in this research. The surface thickness was confirmed by surface plasmon resonance spectroscopy, and the morphology of surface was investigated with scanning tunneling microscopy. The redox property of immobilized myoglobin via chemical linkers having with lengths was carried out by cyclic voltammetry. The redox peaks were shifted due to the incremental length of chemical linkers because electron transfer between myoglobin and gold surface was interrupted by these materials as a capacitor. In these results, it could be applied to regulate redox property of biomolecule for realizing bioelectronic devices. Acknowledgement: This research was supported by The Nano/Bio Science&Technology Program(M10536090001-05N3609-00110) of the Ministry of Education, Science and Technology (MEST), by the Original Technology Research Program for Brain Science through the National Research Foundation of Korea(NRF) funded by the Ministry of Education, Science and Technology (2009-0093907), by the Korea Science and Engineering Foundation (KOSEF) grant funded by the Korea government (MEST) (2010-0000845).
Yong-Ho CHUNG [ Dept. of Chemical & Biomolecular Engineering, Sogang University, Seoul, 121-742. ]
Taek LEE [ Dept. of Chemical & Biomolecular Engineering, Sogang University, Seoul, 121-742. ]
Junhong MIN [ College of Bionanotechnology, Kyungwon University, 461-701. ]
Jeong-Woo CHOI [ Department of Chemical & Biomolecular Engineering and Interdisciplinary Program of Integrated Biotechnology, Sogang University, 121-742. ]
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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