Incorporation of native antibodies and Fc-fusion proteins on DNA nanostructures via a modular conjugation strategy. Rosier, B. J H M, Cremers, G. A O, Engelen, W., Merkx, M., Brunsveld, L., & de Greef, T. F A Chem Commun (Camb), 53(53):7393–7396, June, 2017. abstract bibtex 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.
@ARTICLE{Rosier2017-xn,
title = "Incorporation of native antibodies and Fc-fusion proteins on
{DNA} nanostructures via a modular conjugation strategy",
author = "Rosier, Bas J H M and Cremers, Glenn A O and Engelen, Wouter and
Merkx, Maarten and Brunsveld, Luc and de Greef, Tom F A",
abstract = "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.",
journal = "Chem Commun (Camb)",
volume = 53,
number = 53,
pages = "7393--7396",
month = jun,
year = 2017,
language = "en"
}
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