Author
Listed:
- Daishi Fujita
(School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.)
- Kosuke Suzuki
(School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.)
- Sota Sato
(School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.)
- Maho Yagi-Utsumi
(Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi 444-8787, Japan.
Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, Aichi 467-8603, Japan.)
- Yoshiki Yamaguchi
(RIKEN, Advanced Science Institute, Systems Glycobiology Research Group, Structural Glycobiology Team, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.)
- Nobuhiro Mizuno
(Japan Synchrotron Radiation Research Institute (JASRI/SPring-8), 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.)
- Takashi Kumasaka
(Japan Synchrotron Radiation Research Institute (JASRI/SPring-8), 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.)
- Masaki Takata
(RIKEN SPring-8 Center, RIKEN 1-1-1 Kouto, Sayo-cho, Sayo-gun)
- Masanori Noda
(Graduate School of Engineering, Osaka University
U-Medico Corporation, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.)
- Susumu Uchiyama
(Graduate School of Engineering, Osaka University
U-Medico Corporation, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.)
- Koichi Kato
(Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki, Aichi 444-8787, Japan.
Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya, Aichi 467-8603, Japan.
Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation (JST))
- Makoto Fujita
(School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation (JST))
Abstract
Protein encapsulation has long attracted many chemists and biologists because of its potential to control the structure and functions of proteins, but has been a daunting challenge because of their incommensurably larger size compared with common synthetic hosts. Here we report the encapsulation of a small protein, ubiquitin, within giant coordination cages. The protein was attached to one bidentate ligand and, upon addition of Pd(II) ions (M) and additional ligands (L), M12L24 coordination nanocages self-assembled around the protein. Because of the well-defined host framework, the protein-encapsulated structure could be analysed by NMR spectroscopy, ultracentrifugation and X-ray crystallography.
Suggested Citation
Daishi Fujita & Kosuke Suzuki & Sota Sato & Maho Yagi-Utsumi & Yoshiki Yamaguchi & Nobuhiro Mizuno & Takashi Kumasaka & Masaki Takata & Masanori Noda & Susumu Uchiyama & Koichi Kato & Makoto Fujita, 2012.
"Protein encapsulation within synthetic molecular hosts,"
Nature Communications, Nature, vol. 3(1), pages 1-7, January.
Handle:
RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms2093
DOI: 10.1038/ncomms2093
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