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dc.contributor.author
Richter, Daniel
dc.contributor.author
Lakis, Edgars
dc.contributor.author
Piel, Jörn
dc.date.accessioned
2023-10-05T13:16:16Z
dc.date.available
2023-10-04T07:32:19Z
dc.date.available
2023-10-05T13:16:16Z
dc.date.issued
2023-10
dc.identifier.issn
1755-4349
dc.identifier.issn
1755-4330
dc.identifier.other
10.1038/s41557-023-01252-8
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/634923
dc.identifier.doi
10.3929/ethz-b-000634923
dc.description.abstract
The tetrazine ligation is an inverse electron-demand Diels–Alder reaction widely used for bioorthogonal modifications due to its versatility, site specificity and fast reaction kinetics. A major limitation has been the incorporation of dienophiles in biomolecules and organisms, which relies on externally added reagents. Available methods require the incorporation of tetrazine-reactive groups by enzyme-mediated ligations or unnatural amino acid incorporation. Here we report a tetrazine ligation strategy, termed TyrEx (tyramine excision) cycloaddition, permitting autonomous dienophile generation in bacteria. It utilizes a unique aminopyruvate unit introduced by post-translational protein splicing at a short tag. Tetrazine conjugation occurs rapidly with a rate constant of 0.625 (15) M−1 s−1 and was applied to produce a radiolabel chelator-modified Her2-binding Affibody and intracellular, fluorescently labelled cell division protein FtsZ. We anticipate the labelling strategy to be useful for intracellular studies of proteins, as a stable conjugation method for protein therapeutics, as well as other applications.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Nature
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Site-specific bioorthogonal protein labelling by tetrazine ligation using endogenous β-amino acid dienophiles
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2023-07-03
ethz.journal.title
Nature Chemistry
ethz.journal.volume
15
en_US
ethz.journal.issue
10
en_US
ethz.journal.abbreviated
Nat Chem
ethz.pages.start
1422
en_US
ethz.pages.end
1430
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
Tailored chemical complexity through evolution-inspired synthetic biology
en_US
ethz.grant
A single-cell bacterial synthetic biology platform for the biosynthesis and screening of protease-inhibitory peptide drug leads
en_US
ethz.identifier.scopus
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02520 - Institut für Mikrobiologie / Institute of Microbiology::03980 - Piel, Jörn / Piel, Jörn
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02520 - Institut für Mikrobiologie / Institute of Microbiology::03980 - Piel, Jörn / Piel, Jörn
ethz.grant.agreementno
742739
ethz.grant.agreementno
ETH-21 21-2
ethz.grant.fundername
EC
ethz.grant.fundername
ETHZ
ethz.grant.funderDoi
10.13039/501100000780
ethz.grant.funderDoi
10.13039/501100003006
ethz.grant.program
H2020
ethz.grant.program
ETH Grants
ethz.date.deposited
2023-10-04T07:32:20Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2023-10-05T13:16:17Z
ethz.rosetta.lastUpdated
2024-02-03T04:30:11Z
ethz.rosetta.versionExported
true
ethz.COinS
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