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Ultrafast and selective labeling of endogenous proteins using affinity-based benzotriazole chemistry
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Division of Physiological Chemistry I, Chemical Proteomics Core Facility, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden; Chemical Proteomics, Science for Life Laboratory (SciLifeLab), Stockholm, Sweden.
Division of Physiological Chemistry I, Chemical Proteomics Core Facility, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm 17177, Sweden;Chemical Proteomics, Science for Life Laboratory (SciLifeLab), Stockholm, Sweden.
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2022 (English)In: Chemical Science, ISSN 2041-6520, E-ISSN 2041-6539, Vol. 13, no 24, p. 7240-7246Article in journal (Refereed) Published
Abstract [en]

Chemical modification of proteins is enormously useful for characterizing protein function in complex biological systems and for drug development. Selective labeling of native or endogenous proteins is challenging owing to the existence of distinct functional groups in proteins and in living systems. Chemistry for rapid and selective labeling of proteins remains in high demand. Here we have developed novel affinity labeling probes using benzotriazole (BTA) chemistry. We showed that affinity-based BTA probes selectively and covalently label a lysine residue in the vicinity of the ligand binding site of a target protein with a reaction half-time of 28 s. The reaction rate constant is comparable to the fastest biorthogonal chemistry. This approach was used to selectively label different cytosolic and membrane proteins in vitro and in live cells. BTA chemistry could be widely useful for labeling of native/endogenous proteins, target identification and development of covalent inhibitors.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2022. Vol. 13, no 24, p. 7240-7246
Keywords [en]
affinity labeling, benzotriazole, inhibitors, ligand-directed chemistry, protein modifications
National Category
Biochemistry and Molecular Biology Other Chemistry Topics Organic Chemistry
Research subject
biological chemistry
Identifiers
URN: urn:nbn:se:umu:diva-199553DOI: 10.1039/d1sc05974bISI: 000806432100001PubMedID: 35799822Scopus ID: 2-s2.0-85131868228OAI: oai:DiVA.org:umu-199553DiVA, id: diva2:1697118
Funder
Knut and Alice Wallenberg FoundationGöran Gustafsson Foundation for Research in Natural Sciences and MedicineSwedish Research Council, 2018-04585EU, Horizon 2020, ChemBioAPScience for Life Laboratory, SciLifeLabAvailable from: 2022-09-20 Created: 2022-09-20 Last updated: 2022-09-20Bibliographically approved

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Xin, XiaoyiZhang, YuCorkery, Dale P.Wu, Yao-Wen

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