Protein encapsulation within synthetic molecular hosts

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

doi:10.1038/ncomms2093

Protein encapsulation within synthetic molecular hosts

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

Research output: Contribution to journal › Article › peer-review

164 Citations (Scopus)

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), M 12 L 24 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.

Original language	English
Article number	1093
Journal	Nature communications
Volume	3
DOIs	https://doi.org/10.1038/ncomms2093
Publication status	Published - 2012

ASJC Scopus subject areas

Chemistry(all)
Biochemistry, Genetics and Molecular Biology(all)
General
Physics and Astronomy(all)

Access to Document

10.1038/ncomms2093

Cite this

@article{91f14c64f7e8454fa0bcad553d1ca3ac,

title = "Protein encapsulation within synthetic molecular hosts",

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), M 12 L 24 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.",

author = "Daishi Fujita and Kosuke Suzuki and Sota Sato and Maho Yagi-Utsumi and Yoshiki Yamaguchi and Nobuhiro Mizuno and Takashi Kumasaka and Masaki Takata and Masanori Noda and Susumu Uchiyama and Koichi Kato and Makoto Fujita",

note = "Funding Information: This work was supported by the CREST project of the Japan Science and Technology Agency (JST), the MEXT Grant-in-Aids for Scientific Research for Young Scientists (A) (21685007), Grants-in-Aid for Scientific Research on Innovative Areas (20107004), and Global COE Program (Chemistry Innovation through Cooperation of Science and Engineering), MEXT, Japan. The experiments of synchrotron X-ray crystallography were performed at the BL41XU beamline in the SPring-8 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) (proposal no. 2011B0042), at the BL38B1 beamline in the SPring-8 with the approval of the JASRI (proposal no. 2010B1423, 2011A1102, 2011A1992 and 2011B0039), at the BL26B1 and BL26B2 beamlines in theSPring-8 with the approval of the JASRI (proposal no. 2011A1933) as the Priority Program for Disaster-Affected Quantum Beam Facilities, and at the NE3A and BL17A beamlines in the PF-AR with the approval of the High Energy Accelerator Research Organization (KEK) (proposal no. 2009G502 and 2011G522).",

year = "2012",

doi = "10.1038/ncomms2093",

language = "English",

volume = "3",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "Nature Publishing Group",

}

TY - JOUR

T1 - Protein encapsulation within synthetic molecular hosts

AU - Fujita, Daishi

AU - Suzuki, Kosuke

AU - Sato, Sota

AU - Yagi-Utsumi, Maho

AU - Yamaguchi, Yoshiki

AU - Mizuno, Nobuhiro

AU - Kumasaka, Takashi

AU - Takata, Masaki

AU - Noda, Masanori

AU - Uchiyama, Susumu

AU - Kato, Koichi

AU - Fujita, Makoto

N1 - Funding Information: This work was supported by the CREST project of the Japan Science and Technology Agency (JST), the MEXT Grant-in-Aids for Scientific Research for Young Scientists (A) (21685007), Grants-in-Aid for Scientific Research on Innovative Areas (20107004), and Global COE Program (Chemistry Innovation through Cooperation of Science and Engineering), MEXT, Japan. The experiments of synchrotron X-ray crystallography were performed at the BL41XU beamline in the SPring-8 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) (proposal no. 2011B0042), at the BL38B1 beamline in the SPring-8 with the approval of the JASRI (proposal no. 2010B1423, 2011A1102, 2011A1992 and 2011B0039), at the BL26B1 and BL26B2 beamlines in theSPring-8 with the approval of the JASRI (proposal no. 2011A1933) as the Priority Program for Disaster-Affected Quantum Beam Facilities, and at the NE3A and BL17A beamlines in the PF-AR with the approval of the High Energy Accelerator Research Organization (KEK) (proposal no. 2009G502 and 2011G522).

PY - 2012

Y1 - 2012

N2 - 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), M 12 L 24 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.

AB - 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), M 12 L 24 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.

UR - http://www.scopus.com/inward/record.url?scp=84869380483&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84869380483&partnerID=8YFLogxK

U2 - 10.1038/ncomms2093

DO - 10.1038/ncomms2093

M3 - Article

C2 - 23033069

AN - SCOPUS:84869380483

SN - 2041-1723

VL - 3

JO - Nature Communications

JF - Nature Communications

M1 - 1093

ER -

Protein encapsulation within synthetic molecular hosts

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this