6533b838fe1ef96bd12a3cf6
RESEARCH PRODUCT
Site-Specific Dual Labeling of Proteins on Cysteine Residues with Chlorotetrazines
Claire BernhardMathieu MoreauAlexandra OudotVictor GoncalvesMélanie GuilleminFranck DenatColine Canovassubject
Fluorescence-lifetime imaging microscopyTetrazolesbioconjugation010402 general chemistry01 natural sciencesCatalysisMicesite-specific labelingAnimalsHumans[CHIM]Chemical SciencesTissue DistributionAmino Acid SequenceAminescysteineSerum AlbuminDual labelingFluorescent Dyeschemistry.chemical_classificationBioconjugation010405 organic chemistryBiomoleculeOptical Imagingprotein engineeringGeneral MedicineGeneral ChemistryProtein engineeringFluorescence0104 chemical scienceschemistryBiochemistryclick chemistryClick chemistryPeptidesCysteinedescription
International audience; 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2018-08-13 |