Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic

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Standard

Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic. / Lou, Chenguang; Martos-Maldonado, Manuel C.; Madsen, Charlotte Stahl; Thomsen, Rasmus P.; Midtgaard, Søren Roi; Christensen, Niels Johan; Kjems, Jørgen; Thulstrup, Peter W.; Wengel, Jesper; Jensen, Knud J.

In: Nature Communications, Vol. 7, 12294, 28.07.2016.

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

Harvard

Lou, C, Martos-Maldonado, MC, Madsen, CS, Thomsen, RP, Midtgaard, SR, Christensen, NJ, Kjems, J, Thulstrup, PW, Wengel, J & Jensen, KJ 2016, 'Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic', Nature Communications, vol. 7, 12294. https://doi.org/10.1038/ncomms12294

APA

Lou, C., Martos-Maldonado, M. C., Madsen, C. S., Thomsen, R. P., Midtgaard, S. R., Christensen, N. J., ... Jensen, K. J. (2016). Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic. Nature Communications, 7, [12294]. https://doi.org/10.1038/ncomms12294

CBE

Lou C, Martos-Maldonado MC, Madsen CS, Thomsen RP, Midtgaard SR, Christensen NJ, Kjems J, Thulstrup PW, Wengel J, Jensen KJ. 2016. Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic. Nature Communications. 7. https://doi.org/10.1038/ncomms12294

MLA

Vancouver

Lou C, Martos-Maldonado MC, Madsen CS, Thomsen RP, Midtgaard SR, Christensen NJ et al. Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic. Nature Communications. 2016 Jul 28;7. 12294. https://doi.org/10.1038/ncomms12294

Author

Lou, Chenguang ; Martos-Maldonado, Manuel C. ; Madsen, Charlotte Stahl ; Thomsen, Rasmus P. ; Midtgaard, Søren Roi ; Christensen, Niels Johan ; Kjems, Jørgen ; Thulstrup, Peter W. ; Wengel, Jesper ; Jensen, Knud J. / Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic. In: Nature Communications. 2016 ; Vol. 7.

Bibtex

@article{5963863408644807acc9614d2c2d8f78,
title = "Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic",
abstract = "Peptide-based structures can be designed to yield artificial proteins with specific folding patterns and functions. Template-based assembly of peptide units is one design option, but the use of two orthogonal self-Assembly principles, oligonucleotide triple helix and a coiled coil protein domain formation have never been realized for de novo protein design. Here, we show the applicability of peptide-oligonucleotide conjugates for self-Assembly of higher-ordered protein-like structures. The resulting nano-Assemblies were characterized by ultraviolet-melting, gel electrophoresis, circular dichroism (CD) spectroscopy, small-Angle X-ray scattering and transmission electron microscopy. These studies revealed the formation of the desired triple helix and coiled coil domains at low concentrations, while a dimer of trimers was dominating at high concentration. CD spectroscopy showed an extraordinarily high degree of α-helicity for the peptide moieties in the assemblies. The results validate the use of orthogonal self-Assembly principles as a paradigm for de novo protein design.",
author = "Chenguang Lou and Martos-Maldonado, {Manuel C.} and Madsen, {Charlotte Stahl} and Thomsen, {Rasmus P.} and Midtgaard, {S{\o}ren Roi} and Christensen, {Niels Johan} and J{\o}rgen Kjems and Thulstrup, {Peter W.} and Jesper Wengel and Jensen, {Knud J.}",
year = "2016",
month = "7",
day = "28",
doi = "10.1038/ncomms12294",
language = "English",
volume = "7",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Peptide-oligonucleotide conjugates as nanoscale building blocks for assembly of an artificial three-helix protein mimic

AU - Lou, Chenguang

AU - Martos-Maldonado, Manuel C.

AU - Madsen, Charlotte Stahl

AU - Thomsen, Rasmus P.

AU - Midtgaard, Søren Roi

AU - Christensen, Niels Johan

AU - Kjems, Jørgen

AU - Thulstrup, Peter W.

AU - Wengel, Jesper

AU - Jensen, Knud J.

PY - 2016/7/28

Y1 - 2016/7/28

N2 - Peptide-based structures can be designed to yield artificial proteins with specific folding patterns and functions. Template-based assembly of peptide units is one design option, but the use of two orthogonal self-Assembly principles, oligonucleotide triple helix and a coiled coil protein domain formation have never been realized for de novo protein design. Here, we show the applicability of peptide-oligonucleotide conjugates for self-Assembly of higher-ordered protein-like structures. The resulting nano-Assemblies were characterized by ultraviolet-melting, gel electrophoresis, circular dichroism (CD) spectroscopy, small-Angle X-ray scattering and transmission electron microscopy. These studies revealed the formation of the desired triple helix and coiled coil domains at low concentrations, while a dimer of trimers was dominating at high concentration. CD spectroscopy showed an extraordinarily high degree of α-helicity for the peptide moieties in the assemblies. The results validate the use of orthogonal self-Assembly principles as a paradigm for de novo protein design.

AB - Peptide-based structures can be designed to yield artificial proteins with specific folding patterns and functions. Template-based assembly of peptide units is one design option, but the use of two orthogonal self-Assembly principles, oligonucleotide triple helix and a coiled coil protein domain formation have never been realized for de novo protein design. Here, we show the applicability of peptide-oligonucleotide conjugates for self-Assembly of higher-ordered protein-like structures. The resulting nano-Assemblies were characterized by ultraviolet-melting, gel electrophoresis, circular dichroism (CD) spectroscopy, small-Angle X-ray scattering and transmission electron microscopy. These studies revealed the formation of the desired triple helix and coiled coil domains at low concentrations, while a dimer of trimers was dominating at high concentration. CD spectroscopy showed an extraordinarily high degree of α-helicity for the peptide moieties in the assemblies. The results validate the use of orthogonal self-Assembly principles as a paradigm for de novo protein design.

U2 - 10.1038/ncomms12294

DO - 10.1038/ncomms12294

M3 - Journal article

C2 - 27464951

AN - SCOPUS:84979914245

VL - 7

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 12294

ER -