Protein encapsulation within synthetic molecular hosts
2012; Nature Portfolio; Volume: 3; Issue: 1 Linguagem: Inglês
10.1038/ncomms2093
ISSN2041-1723
AutoresDaishi Fujita, Kosuke Suzuki, Sota Sato, Maho Yagi‐Utsumi, Yoshiki Yamaguchi, Nobuhiro Mizuno, Takashi Kumasaka, Masaki Takata, Masanori Noda, Susumu Uchiyama, Koichi Kato, Makoto Fujita,
Tópico(s)Supramolecular Chemistry and Complexes
ResumoProtein 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. Protein encapsulation in molecular cages has the potential to alter protein function and aid crystallization. Here, ubiquitin is encapsulated within a giant coordination cage; the protein is attached to a bidentate ligand, and the cage self-assembles upon addition of capping ligands and Pd(II) ions.
Referência(s)