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dc.contributor.author
Cremers, Glenn A.O.
dc.contributor.author
Rosier, Bas J.H.M.
dc.contributor.author
Meijs, Ab
dc.contributor.author
Tito, Nicholas B.
dc.contributor.author
van Duijnhoven, Sander M.J.
dc.contributor.author
van Eenennaam, Hans
dc.contributor.author
Albertazzi, Lorenzo
dc.contributor.author
De Greef, Tom F.A.
dc.date.accessioned
2021-08-02T15:27:51Z
dc.date.available
2021-08-01T19:50:39Z
dc.date.available
2021-08-02T15:27:51Z
dc.date.issued
2021-07-14
dc.identifier.issn
0002-7863
dc.identifier.issn
1520-5126
dc.identifier.other
10.1021/jacs.1c02298
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/498818
dc.identifier.doi
10.3929/ethz-b-000498818
dc.description.abstract
Synthesis of ligand-functionalized nanomaterials with control over size, shape, and ligand orientation facilitates the design of targeted nanomedicines for therapeutic purposes. DNA nanotechnology has emerged as a powerful tool to rationally construct two- and three-dimensional nanostructures, enabling site-specific incorporation of protein ligands with control over stoichiometry and orientation. To efficiently target cell surface receptors, exploration of the parameters that modulate cellular accessibility of these nanostructures is essential. In this study, we systematically investigate tunable design parameters of antibody-functionalized DNA nanostructures binding to therapeutically relevant receptors, including the programmed cell death protein 1, the epidermal growth factor receptor, and the human epidermal growth factor receptor 2. We show that, although the native affinity of antibody-functionalized DNA nanostructures remains unaltered, the absolute number of bound surface receptors is lower compared to soluble antibodies due to receptor accessibility by the nanostructure. We explore structural determinants of this phenomenon to improve efficiency, revealing that receptor binding is mainly governed by nanostructure size and DNA handle location. The obtained results provide key insights in the ability of ligand-functionalized DNA nanostructures to bind surface receptors and yields design rules for optimal cellular targeting.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
American Chemical Society
en_US
dc.rights.uri
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.title
Determinants of Ligand-Functionalized DNA Nanostructure-Cell Interactions
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
dc.date.published
2021-06-28
ethz.journal.title
Journal of the American Chemical Society
ethz.journal.volume
143
en_US
ethz.journal.issue
27
en_US
ethz.journal.abbreviated
J. Am. Chem. Soc.
ethz.pages.start
10131
en_US
ethz.pages.end
10142
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Washington, DC
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02350 - Dep. Umweltsystemwissenschaften / Dep. of Environmental Systems Science::02721 - Inst. f. Biogeochemie u. Schadstoffdyn. / Inst. Biogeochem. and Pollutant Dynamics::03850 - McNeill, Kristopher / McNeill, Kristopher
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02350 - Dep. Umweltsystemwissenschaften / Dep. of Environmental Systems Science::02721 - Inst. f. Biogeochemie u. Schadstoffdyn. / Inst. Biogeochem. and Pollutant Dynamics::03850 - McNeill, Kristopher / McNeill, Kristopher
ethz.date.deposited
2021-08-01T19:51:38Z
ethz.source
WOS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2021-08-02T15:27:58Z
ethz.rosetta.lastUpdated
2022-03-29T10:53:11Z
ethz.rosetta.versionExported
true
ethz.COinS
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