Lainšček, Duško

Link to this page

Authority KeyName Variants
363c9d9f-77be-4382-8fe2-3f154c4f219d
  • Lainšček, Duško (1)
Projects

Author's Bibliography

Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo

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

(Nature Publishing Group, New York, 2017)

TY  - 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 . .
126
144
85
122
130