Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo
Author(s) -
Ajasja Ljubetič,
Fabio Lapenta,
Helena Gradišar,
Igor Drobnak,
Jana Aupič,
Žiga Strmšek,
Duško Lainšček,
Iva HafnerBratkovič,
Andreja Majerle,
Nuša Krivec,
Mojca Benčina,
Tomaž Pisanski,
Tanja Ćirković Veličković,
Adam Round,
J.M. Carazo,
Roberto Melero,
Roman Jerala
Publication year - 2017
Publication title -
nature biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 15.358
H-Index - 445
eISSN - 1546-1696
pISSN - 1087-0156
DOI - 10.1038/nbt.3994
Subject(s) - protein design , folding (dsp implementation) , coiled coil , in vivo , protein folding , protein structure , crystallography , protein engineering , biophysics , tetrahedron , chemistry , nanotechnology , materials science , biology , biochemistry , enzyme , microbiology and biotechnology , electrical engineering , engineering
Polypeptides and polynucleotides are natural programmable biopolymers that can self-assemble into complex tertiary structures. We describe a system analogous to designed DNA nanostructures in which protein coiled-coil (CC) dimers serve as building blocks for modular de novo design of polyhedral protein cages that efficiently self-assemble in vitro and in vivo. We produced and characterized >20 single-chain protein cages in three shapes-tetrahedron, four-sided pyramid, and triangular prism-with the largest containing >700 amino-acid residues and measuring 11 nm in diameter. Their stability and folding kinetics were similar to those of natural proteins. Solution small-angle X-ray scattering (SAXS), electron microscopy (EM), and biophysical analysis confirmed agreement of the expressed structures with the designs. We also demonstrated self-assembly of a tetrahedral structure in bacteria, mammalian cells, and mice without evidence of inflammation. A semi-automated computational design platform and a toolbox of CC building modules are provided to enable the design of protein cages in any polyhedral shape.
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