한빛사 논문
Yuseung Jo 1∞, Jin Seok Woo 2∞, A Ram Lee 2 3, Seon-Yeong Lee 2, Yonghee Shin 1, Luke P Lee 4 5 6, Mi-La Cho 3 7*, Taewook Kang 1 8*
1Department of Chemical and Biomolecular Engineering, Sogang University, Seoul 04107, Korea.
2Rheumatism Research Center, College of Medicine, Catholic Research Institute of Medical Science, The Catholic University of Korea, Seoul 06591, Korea.
3Department of Biomedicine & Health Sciences, College of Medicine, The Catholic University of Korea, Seoul 06591, Korea.
4Harvard Medical School, Harvard University; Renal Division and Division of Engineering in Medicine, Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts 02115, United States.
5Department of Bioengineering, and Department of Electrical Engineering and Computer Science, University of California, Berkeley, Berkeley, California 94720, United States.
6Institute of Quantum Biophysics, Department of Biophysics, Sungkyunkwan University, Suwon 16419, Korea.
7Department of Medical Life Scieneces, College of Medicine, The Catholic University of Korea, Seoul 06591, Korea.
8Institute of Integrated Biotechnology, Sogang University, Seoul 04107, Korea.
∞ Y.J. and J.S.W. contributed equally to the work.
*Corresponding Authors: Mi-La Cho, Taewook Kang
Abstract
Electron transfer through the mitochondrial electron transport chain (ETC) can be critically blocked by the dysfunction of protein complexes. Redox-active molecules have been used to mediate the electron transfer in place of the dysfunctional complexes; however, they are limited to replacing complex I and are known to be toxic. Here we report artificial mitochondrial electron transfer pathways that enhance ETC activity by exploiting inner-membrane-bound gold nanoparticles (GNPs) as efficient electron transfer mediators. The hybridization of mitochondria with GNPs, driven by electrostatic interaction, is successfully visualized in real time at the level of a single mitochondrion. By observing quantized quenching dips via plasmon resonance energy transfer, we reveal that the hybridized GNPs are bound to the inner membrane of mitochondria irrespective of the presence of the outer membrane. The ETC activity of mitochondria with GNPs such as membrane potential, oxygen consumption, and ATP production is remarkably increased <i>in vitro</i>.
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