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Frontispiece: Highly Stable trans ‐Cyclooctene Amino Acids for Live‐Cell Labeling
Author(s) -
Hoffmann JanErik,
Plass Tilman,
Nikić Ivana,
Aramburu Iker Valle,
Koehler Christine,
Gillandt Hartmut,
Lemke Edward A.,
Schultz Carsten
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201583561
Subject(s) - click chemistry , tetrazine , chemistry , reactivity (psychology) , amino acid , lysine , bioorthogonal chemistry , cyclooctene , combinatorial chemistry , biochemistry , organic chemistry , catalysis , medicine , alternative medicine , pathology
Amino Acids for Live‐Cell Labeling . The non‐canonical amino acid trans ‐cyclooctene‐lysine (TCO*) allows the rapid and specific labeling of proteins by click chemistry. In their Communication on page 12266 ff. , C. Schultz et al. present a novel synthesis route for TCO* and investigate the stability and reactivity of the isomers, as well as their utility for live‐cell labeling. The reactivity of TCO* conformers with tetrazines in comparison to other common click reactions is systematically quantified by using density functional calculations. The axial isomer of TCO* incorporated in a green fluorescent protein reacts with a tetrazine attached to Cy5. The relevant orbitals involved in this extremely fast click reaction are shown on a background of mammalian cells expressing insulin receptors selectively labeled by this method.