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dc.contributor.author
Pellegrino, Christian
dc.contributor.author
Favalli, Nicholas
dc.contributor.author
Sandholzer, Michael
dc.contributor.author
Volta, Laura
dc.contributor.author
Bassi, Gabriele
dc.contributor.author
Millul, Jacopo
dc.contributor.author
Cazzamalli, Samuele
dc.contributor.author
Matasci, Mattia
dc.contributor.author
Villa, Alessandra
dc.contributor.author
Myburgh, Renier
dc.contributor.author
Manz, Markus G.
dc.contributor.author
Neri, Dario
dc.date.accessioned
2020-07-30T10:10:04Z
dc.date.available
2020-07-25T22:32:41Z
dc.date.available
2020-07-30T10:10:04Z
dc.date.issued
2020-07-15
dc.identifier.issn
1043-1802
dc.identifier.issn
1520-4812
dc.identifier.other
10.1021/acs.bioconjchem.0c00258
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/428469
dc.description.abstract
All Universal Chimeric Antigen Receptor T-cells (UniCAR T-cells) are T-cells which have been engineered to recognize a haptenated ligand. Due to this feature, UniCAR T-cells have the potential to mediate a potent and selective tumor killing only in the presence of a haptenated tumor ligand, thus avoiding the long-lasting biocidal effects of conventional CAR T-cells. We have used fluorescein-labeled versions of small organic ligands and different antibody formats specific to carbonic anhydrase IX (a tumor-associated antigen) in order to assess whether the killing potential of UniCAR T-cells depended on the molecular features of the haptenated molecule. Both small molecule ligands and larger antibody fragments were potent in mediating tumor cell killing over a broad concentration range. Antibodies could be conveniently used both in IgG format and as smaller diabody fragments. Importantly, the use of site-specific chemical modification strategies for the antibody coupling to fluorescein led to a substantial improvement of tumor cell killing performance, compared to the random modification of primary amino groups on the antibody surface.
en_US
dc.language.iso
en
en_US
dc.publisher
American Chemical Society
en_US
dc.subject
Immunology
en_US
dc.subject
Peptides and proteins
en_US
dc.subject
Fluorescence
en_US
dc.subject
Cells
en_US
dc.subject
Biopolymers
en_US
dc.title
Impact of Ligand Size and Conjugation Chemistry on the Performance of Universal Chimeric Antigen Receptor T-Cells for Tumor Killing
en_US
dc.type
Journal Article
dc.date.published
2020-06-09
ethz.journal.title
Bioconjugate Chemistry
ethz.journal.volume
31
en_US
ethz.journal.issue
7
en_US
ethz.journal.abbreviated
Bioconjug. chem.
ethz.pages.start
1775
en_US
ethz.pages.end
1783
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Columbus, OH
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02534 - Institut für Pharmazeutische Wiss. / Institute of Pharmaceutical Sciences::03463 - Neri, Dario (ehemalig) / Neri, Dario (former)
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02534 - Institut für Pharmazeutische Wiss. / Institute of Pharmaceutical Sciences::03463 - Neri, Dario (ehemalig) / Neri, Dario (former)
ethz.relation.isPartOf
10.3929/ethz-b-000462500
ethz.date.deposited
2020-07-25T22:33:09Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Metadata only
en_US
ethz.rosetta.installDate
2020-07-30T10:10:15Z
ethz.rosetta.lastUpdated
2022-03-29T02:43:40Z
ethz.rosetta.versionExported
true
ethz.COinS
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