Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo
Samo za registrovane korisnike
2017
Autori
Ljubetič, AjasjaLapenta, Fabio
Gradišar, Helena
Drobnak, Igor
Aupič, Jana
Strmšek, Žiga
Lainšček, Duško
Hafner-Bratkovič, Iva
Majerle, Andreja
Krivec, Nuša
Benčina, Mojca
Pisanski, Tomaž
Ćirković-Veličković, Tanja
Round, Adam
José María Carazo
Melero, Roberto
Jerala, Roman
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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 gt 20 single-chain protein cages in three shapes-tetrahedron, four-sided pyramid, and triangular prism-with the largest containing gt 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 desig...n platform and a toolbox of CC building modules are provided to enable the design of protein cages in any polyhedral shape.
Izvor:
Nature Biotechnology, 2017, 35, 11, 1094-Izdavač:
- Nature Publishing Group, New York
Finansiranje / projekti:
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-FP7-256716)
- Slovenian Research Agency [P4-0176, N4-0037, J4-5528, L4-6812, J3-7034, BI-US/17-18-051]
- NVIDIA Corporation for the donation of the Quadro [GP100 GPU]
- ERANET SynBio project Bioorigami [ERASYNBIO1-006]
- ICGEB [CRP/SLO14-03]
- iNEXT - Horizon 2020 Programme of the EU [PID1771, PID2706, PID1824, VID3987]
- COST actions [CM1304, CM1306]
Napomena:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3212
DOI: 10.1038/nbt.3994
ISSN: 1087-0156
PubMed: 29035374
WoS: 000414856200026
Scopus: 2-s2.0-85033600678
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Ljubetič, Ajasja AU - Lapenta, Fabio AU - Gradišar, Helena AU - Drobnak, Igor AU - Aupič, Jana AU - Strmšek, Žiga AU - Lainšček, Duško AU - Hafner-Bratkovič, Iva AU - Majerle, Andreja AU - Krivec, Nuša AU - Benčina, Mojca AU - Pisanski, Tomaž AU - Ćirković-Veličković, Tanja AU - Round, Adam AU - José María Carazo AU - Melero, Roberto AU - Jerala, Roman PY - 2017 UR - https://cherry.chem.bg.ac.rs/handle/123456789/2549 AB - 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 gt 20 single-chain protein cages in three shapes-tetrahedron, four-sided pyramid, and triangular prism-with the largest containing gt 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. PB - Nature Publishing Group, New York T2 - Nature Biotechnology T1 - Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo VL - 35 IS - 11 SP - 1094 DO - 10.1038/nbt.3994 ER -
@article{ author = "Ljubetič, Ajasja and Lapenta, Fabio and Gradišar, Helena and Drobnak, Igor and Aupič, Jana and Strmšek, Žiga and Lainšček, Duško and Hafner-Bratkovič, Iva and Majerle, Andreja and Krivec, Nuša and Benčina, Mojca and Pisanski, Tomaž and Ćirković-Veličković, Tanja and Round, Adam and José María Carazo and Melero, Roberto and Jerala, Roman", year = "2017", abstract = "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 gt 20 single-chain protein cages in three shapes-tetrahedron, four-sided pyramid, and triangular prism-with the largest containing gt 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.", publisher = "Nature Publishing Group, New York", journal = "Nature Biotechnology", title = "Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo", volume = "35", number = "11", pages = "1094", doi = "10.1038/nbt.3994" }
Ljubetič, A., Lapenta, F., Gradišar, H., Drobnak, I., Aupič, J., Strmšek, Ž., Lainšček, D., Hafner-Bratkovič, I., Majerle, A., Krivec, N., Benčina, M., Pisanski, T., Ćirković-Veličković, T., Round, A., José María Carazo, Melero, R.,& Jerala, R.. (2017). Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo. in Nature Biotechnology Nature Publishing Group, New York., 35(11), 1094. https://doi.org/10.1038/nbt.3994
Ljubetič A, Lapenta F, Gradišar H, Drobnak I, Aupič J, Strmšek Ž, Lainšček D, Hafner-Bratkovič I, Majerle A, Krivec N, Benčina M, Pisanski T, Ćirković-Veličković T, Round A, José María Carazo, Melero R, Jerala R. Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo. in Nature Biotechnology. 2017;35(11):1094. doi:10.1038/nbt.3994 .
Ljubetič, Ajasja, Lapenta, Fabio, Gradišar, Helena, Drobnak, Igor, Aupič, Jana, Strmšek, Žiga, Lainšček, Duško, Hafner-Bratkovič, Iva, Majerle, Andreja, Krivec, Nuša, Benčina, Mojca, Pisanski, Tomaž, Ćirković-Veličković, Tanja, Round, Adam, José María Carazo, Melero, Roberto, Jerala, Roman, "Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo" in Nature Biotechnology, 35, no. 11 (2017):1094, https://doi.org/10.1038/nbt.3994 . .