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Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Standard

Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins. / Rosen, Christian B; Kodal, Anne L B; Nielsen, Jesper S et al.
I: Nature Chemistry, Bind 6, Nr. 9, 09.2014, s. 804-809.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Rosen, CB, Kodal, ALB, Nielsen, JS, Schaffert, DH, Scavenius, C, Okholm, AH, Voigt, NV, Enghild, JJ, Kjems, J, Tørring, T & Gothelf, KV 2014, 'Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins', Nature Chemistry, bind 6, nr. 9, s. 804-809. https://doi.org/10.1038/nchem.2003

APA

Rosen, C. B., Kodal, A. L. B., Nielsen, J. S., Schaffert, D. H., Scavenius, C., Okholm, A. H., Voigt, N. V., Enghild, J. J., Kjems, J., Tørring, T., & Gothelf, K. V. (2014). Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins. Nature Chemistry, 6(9), 804-809. https://doi.org/10.1038/nchem.2003

CBE

Rosen CB, Kodal ALB, Nielsen JS, Schaffert DH, Scavenius C, Okholm AH, Voigt NV, Enghild JJ, Kjems J, Tørring T, et al. 2014. Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins. Nature Chemistry. 6(9):804-809. https://doi.org/10.1038/nchem.2003

MLA

Rosen, Christian B et al. "Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins". Nature Chemistry. 2014, 6(9). 804-809. https://doi.org/10.1038/nchem.2003

Vancouver

Rosen CB, Kodal ALB, Nielsen JS, Schaffert DH, Scavenius C, Okholm AH et al. Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins. Nature Chemistry. 2014 sep.;6(9):804-809. doi: 10.1038/nchem.2003

Author

Rosen, Christian B ; Kodal, Anne L B ; Nielsen, Jesper S et al. / Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins. I: Nature Chemistry. 2014 ; Bind 6, Nr. 9. s. 804-809.

Bibtex

@article{fad98f3c2b7a414d9d170979cbf659e8,
title = "Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins",
abstract = "DNA-protein conjugates are important in bioanalytical chemistry, molecular diagnostics and bionanotechnology, as the DNA provides a unique handle to identify, functionalize or otherwise manipulate proteins. To maintain protein activity, conjugation of a single DNA handle to a specific location on the protein is often needed. However, preparing such high-quality site-specific conjugates often requires genetically engineered proteins, which is a laborious and technically challenging approach. Here we demonstrate a simpler method to create site-selective DNA-protein conjugates. Using a guiding DNA strand modified with a metal-binding functionality, we directed a second DNA strand to the vicinity of a metal-binding site of His6-tagged or wild-type metal-binding proteins, such as serotransferrin, where it subsequently reacted with lysine residues at that site. This method, DNA-templated protein conjugation, facilitates the production of site-selective protein conjugates, and also conjugation to IgG1 antibodies via a histidine cluster in the constant domain.",
author = "Rosen, {Christian B} and Kodal, {Anne L B} and Nielsen, {Jesper S} and Schaffert, {David H} and Carsten Scavenius and Okholm, {Anders H} and Voigt, {Niels V} and Enghild, {Jan Johannes} and J{\o}rgen Kjems and Thomas T{\o}rring and Gothelf, {Kurt V}",
year = "2014",
month = sep,
doi = "10.1038/nchem.2003",
language = "English",
volume = "6",
pages = "804--809",
journal = "Nature Chemistry",
issn = "1755-4330",
publisher = "Nature Publishing Group",
number = "9",

}

RIS

TY - JOUR

T1 - Template-directed covalent conjugation of DNA to native antibodies, transferrin and other metal-binding proteins

AU - Rosen, Christian B

AU - Kodal, Anne L B

AU - Nielsen, Jesper S

AU - Schaffert, David H

AU - Scavenius, Carsten

AU - Okholm, Anders H

AU - Voigt, Niels V

AU - Enghild, Jan Johannes

AU - Kjems, Jørgen

AU - Tørring, Thomas

AU - Gothelf, Kurt V

PY - 2014/9

Y1 - 2014/9

N2 - DNA-protein conjugates are important in bioanalytical chemistry, molecular diagnostics and bionanotechnology, as the DNA provides a unique handle to identify, functionalize or otherwise manipulate proteins. To maintain protein activity, conjugation of a single DNA handle to a specific location on the protein is often needed. However, preparing such high-quality site-specific conjugates often requires genetically engineered proteins, which is a laborious and technically challenging approach. Here we demonstrate a simpler method to create site-selective DNA-protein conjugates. Using a guiding DNA strand modified with a metal-binding functionality, we directed a second DNA strand to the vicinity of a metal-binding site of His6-tagged or wild-type metal-binding proteins, such as serotransferrin, where it subsequently reacted with lysine residues at that site. This method, DNA-templated protein conjugation, facilitates the production of site-selective protein conjugates, and also conjugation to IgG1 antibodies via a histidine cluster in the constant domain.

AB - DNA-protein conjugates are important in bioanalytical chemistry, molecular diagnostics and bionanotechnology, as the DNA provides a unique handle to identify, functionalize or otherwise manipulate proteins. To maintain protein activity, conjugation of a single DNA handle to a specific location on the protein is often needed. However, preparing such high-quality site-specific conjugates often requires genetically engineered proteins, which is a laborious and technically challenging approach. Here we demonstrate a simpler method to create site-selective DNA-protein conjugates. Using a guiding DNA strand modified with a metal-binding functionality, we directed a second DNA strand to the vicinity of a metal-binding site of His6-tagged or wild-type metal-binding proteins, such as serotransferrin, where it subsequently reacted with lysine residues at that site. This method, DNA-templated protein conjugation, facilitates the production of site-selective protein conjugates, and also conjugation to IgG1 antibodies via a histidine cluster in the constant domain.

U2 - 10.1038/nchem.2003

DO - 10.1038/nchem.2003

M3 - Journal article

C2 - 25143216

VL - 6

SP - 804

EP - 809

JO - Nature Chemistry

JF - Nature Chemistry

SN - 1755-4330

IS - 9

ER -