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Site‐Specific Dual Labeling of Proteins on Cysteine Residues with Chlorotetrazines
Author(s) -
Canovas Coline,
Moreau Mathieu,
Bernhard Claire,
Oudot Alexandra,
Guillemin Mélanie,
Denat Franck,
Goncalves Victor
Publication year - 2018
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201806053
Subject(s) - bioconjugation , biomolecule , cysteine , chemistry , fluorescence , combinatorial chemistry , biochemistry , computational biology , biophysics , biology , physics , quantum mechanics , enzyme
Dual‐labeled biomolecules constitute a new generation of bioconjugates with promising applications in therapy and diagnosis. Unfortunately, the development of these new families of biologics is hampered by the technical difficulties associated with their construction. In particular, the site specificity of the conjugation is critical as the number and position of payloads can have a dramatic impact on the pharmacokinetics of the bioconjugate. Herein, we introduce dichlorotetrazine as a trivalent platform for the selective double modification of proteins on cysteine residues. This strategy is applied to the dual labeling of albumin with a macrocyclic chelator for nuclear imaging and a fluorescent probe for fluorescence imaging.