Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy

A photocrosslinkable protein G variant was used as an adapter protein to covalently and site-specifically conjugate an antibody and an Fc-fusion protein to an oligonucleotide. This modular approach enables straightforward decoration of DNA nanostructures with complex native proteins while retaining...

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Autores principales: Rosier, Bas J. H. M., Cremers, Glenn A. O., Engelen, Wouter, Merkx, Maarten, Brunsveld, Luc, de Greef, Tom F. A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5708335/
https://www.ncbi.nlm.nih.gov/pubmed/28617516
http://dx.doi.org/10.1039/c7cc04178k
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author Rosier, Bas J. H. M.
Cremers, Glenn A. O.
Engelen, Wouter
Merkx, Maarten
Brunsveld, Luc
de Greef, Tom F. A.
author_facet Rosier, Bas J. H. M.
Cremers, Glenn A. O.
Engelen, Wouter
Merkx, Maarten
Brunsveld, Luc
de Greef, Tom F. A.
author_sort Rosier, Bas J. H. M.
collection PubMed
description A photocrosslinkable protein G variant was used as an adapter protein to covalently and site-specifically conjugate an antibody and an Fc-fusion protein to an oligonucleotide. This modular approach enables straightforward decoration of DNA nanostructures with complex native proteins while retaining their innate binding affinity, allowing precise control over the nanoscale spatial organization of such proteins for in vitro and in vivo biomedical applications.
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spelling pubmed-57083352018-01-05 Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy Rosier, Bas J. H. M. Cremers, Glenn A. O. Engelen, Wouter Merkx, Maarten Brunsveld, Luc de Greef, Tom F. A. Chem Commun (Camb) Chemistry A photocrosslinkable protein G variant was used as an adapter protein to covalently and site-specifically conjugate an antibody and an Fc-fusion protein to an oligonucleotide. This modular approach enables straightforward decoration of DNA nanostructures with complex native proteins while retaining their innate binding affinity, allowing precise control over the nanoscale spatial organization of such proteins for in vitro and in vivo biomedical applications. Royal Society of Chemistry 2017-07-07 2017-06-09 /pmc/articles/PMC5708335/ /pubmed/28617516 http://dx.doi.org/10.1039/c7cc04178k Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Rosier, Bas J. H. M.
Cremers, Glenn A. O.
Engelen, Wouter
Merkx, Maarten
Brunsveld, Luc
de Greef, Tom F. A.
Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy
title Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy
title_full Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy
title_fullStr Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy
title_full_unstemmed Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy
title_short Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy
title_sort incorporation of native antibodies and fc-fusion proteins on dna nanostructures via a modular conjugation strategy
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5708335/
https://www.ncbi.nlm.nih.gov/pubmed/28617516
http://dx.doi.org/10.1039/c7cc04178k
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