Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions

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Standard

Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions. / Sprengel, Andreas; Lill, Pascal; Stegemann, Pierre; Bravo-Rodriguez, Kenny; Schöneweiß, Elisa C.; Merdanovic, Melisa; Gudnason, Daniel; Aznauryan, Mikayel; Gamrad, Lisa; Barcikowski, Stephan; Sanchez-Garcia, Elsa; Birkedal, Victoria; Gatsogiannis, Christos; Ehrmann, Michael; Saccà, Barbara.

In: Nature Communications, Vol. 8, 14472 (2017), 2017.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Sprengel, A, Lill, P, Stegemann, P, Bravo-Rodriguez, K, Schöneweiß, EC, Merdanovic, M, Gudnason, D, Aznauryan, M, Gamrad, L, Barcikowski, S, Sanchez-Garcia, E, Birkedal, V, Gatsogiannis, C, Ehrmann, M & Saccà, B 2017, 'Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions', Nature Communications, vol. 8, 14472 (2017). https://doi.org/10.1038/ncomms14472

APA

Sprengel, A., Lill, P., Stegemann, P., Bravo-Rodriguez, K., Schöneweiß, E. C., Merdanovic, M., Gudnason, D., Aznauryan, M., Gamrad, L., Barcikowski, S., Sanchez-Garcia, E., Birkedal, V., Gatsogiannis, C., Ehrmann, M., & Saccà, B. (2017). Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions. Nature Communications, 8, [14472 (2017)]. https://doi.org/10.1038/ncomms14472

CBE

Sprengel A, Lill P, Stegemann P, Bravo-Rodriguez K, Schöneweiß EC, Merdanovic M, Gudnason D, Aznauryan M, Gamrad L, Barcikowski S, Sanchez-Garcia E, Birkedal V, Gatsogiannis C, Ehrmann M, Saccà B. 2017. Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions. Nature Communications. 8:Article 14472 (2017). https://doi.org/10.1038/ncomms14472

MLA

Vancouver

Sprengel A, Lill P, Stegemann P, Bravo-Rodriguez K, Schöneweiß EC, Merdanovic M et al. Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions. Nature Communications. 2017;8. 14472 (2017). https://doi.org/10.1038/ncomms14472

Author

Sprengel, Andreas ; Lill, Pascal ; Stegemann, Pierre ; Bravo-Rodriguez, Kenny ; Schöneweiß, Elisa C. ; Merdanovic, Melisa ; Gudnason, Daniel ; Aznauryan, Mikayel ; Gamrad, Lisa ; Barcikowski, Stephan ; Sanchez-Garcia, Elsa ; Birkedal, Victoria ; Gatsogiannis, Christos ; Ehrmann, Michael ; Saccà, Barbara. / Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions. In: Nature Communications. 2017 ; Vol. 8.

Bibtex

@article{37808a6b28dd4a88ab517939697adc88,
title = "Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions",
abstract = "The self-organizational properties of DNA have been used to realize synthetic hosts for protein encapsulation. However, current strategies of DNA-protein conjugation still limit true emulation of natural host-guest systems, whose formation relies on non-covalent bonds between geometrically matching interfaces. Here we report one of the largest DNA-protein complexes of semisynthetic origin held in place exclusively by spatially defined supramolecular interactions. Our approach is based on the decoration of the inner surface of a DNA origami hollow structure with multiple ligands converging to their corresponding binding sites on the protein surface with programmable symmetry and range-of-action. Our results demonstrate specific host-guest recognition in a 1:1 stoichiometry and selectivity for the guest whose size guarantees sufficient molecular diffusion preserving short intermolecular distances. DNA nanocontainers can be thus rationally designed to trap single guest molecules in their native form, mimicking natural strategies of molecular recognition and anticipating a new method of protein caging.",
author = "Andreas Sprengel and Pascal Lill and Pierre Stegemann and Kenny Bravo-Rodriguez and Sch{\"o}newei{\ss}, {Elisa C.} and Melisa Merdanovic and Daniel Gudnason and Mikayel Aznauryan and Lisa Gamrad and Stephan Barcikowski and Elsa Sanchez-Garcia and Victoria Birkedal and Christos Gatsogiannis and Michael Ehrmann and Barbara Sacc{\`a}",
year = "2017",
doi = "10.1038/ncomms14472",
language = "English",
volume = "8",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions

AU - Sprengel, Andreas

AU - Lill, Pascal

AU - Stegemann, Pierre

AU - Bravo-Rodriguez, Kenny

AU - Schöneweiß, Elisa C.

AU - Merdanovic, Melisa

AU - Gudnason, Daniel

AU - Aznauryan, Mikayel

AU - Gamrad, Lisa

AU - Barcikowski, Stephan

AU - Sanchez-Garcia, Elsa

AU - Birkedal, Victoria

AU - Gatsogiannis, Christos

AU - Ehrmann, Michael

AU - Saccà, Barbara

PY - 2017

Y1 - 2017

N2 - The self-organizational properties of DNA have been used to realize synthetic hosts for protein encapsulation. However, current strategies of DNA-protein conjugation still limit true emulation of natural host-guest systems, whose formation relies on non-covalent bonds between geometrically matching interfaces. Here we report one of the largest DNA-protein complexes of semisynthetic origin held in place exclusively by spatially defined supramolecular interactions. Our approach is based on the decoration of the inner surface of a DNA origami hollow structure with multiple ligands converging to their corresponding binding sites on the protein surface with programmable symmetry and range-of-action. Our results demonstrate specific host-guest recognition in a 1:1 stoichiometry and selectivity for the guest whose size guarantees sufficient molecular diffusion preserving short intermolecular distances. DNA nanocontainers can be thus rationally designed to trap single guest molecules in their native form, mimicking natural strategies of molecular recognition and anticipating a new method of protein caging.

AB - The self-organizational properties of DNA have been used to realize synthetic hosts for protein encapsulation. However, current strategies of DNA-protein conjugation still limit true emulation of natural host-guest systems, whose formation relies on non-covalent bonds between geometrically matching interfaces. Here we report one of the largest DNA-protein complexes of semisynthetic origin held in place exclusively by spatially defined supramolecular interactions. Our approach is based on the decoration of the inner surface of a DNA origami hollow structure with multiple ligands converging to their corresponding binding sites on the protein surface with programmable symmetry and range-of-action. Our results demonstrate specific host-guest recognition in a 1:1 stoichiometry and selectivity for the guest whose size guarantees sufficient molecular diffusion preserving short intermolecular distances. DNA nanocontainers can be thus rationally designed to trap single guest molecules in their native form, mimicking natural strategies of molecular recognition and anticipating a new method of protein caging.

U2 - 10.1038/ncomms14472

DO - 10.1038/ncomms14472

M3 - Journal article

C2 - 28205515

AN - SCOPUS:85013197007

VL - 8

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 14472 (2017)

ER -