6533b7dbfe1ef96bd1270a5a
RESEARCH PRODUCT
Chemoselective Dual Labeling of Native and Recombinant Proteins
Bikram Keshari AgrawallaAndreas RieggerMatthias P. DomogallaMatthias P. DomogallaTao WangXi ChenThilo DörflerTanja WeilFelix BoldtSeah Ling KuanMarkus LamlaJens MichaelisKerstin Steinbrinksubject
0301 basic medicineModels MolecularBiomedical EngineeringPharmaceutical ScienceBioengineering010402 general chemistry01 natural scienceslaw.inventionCell LineMaleimides03 medical and health scienceschemistry.chemical_compoundMiceBacterial ProteinslawAnimalsHumansReactivity (chemistry)CysteineSulfhydryl CompoundsSulfonesMaleimidePeptide sequenceDual labelingPharmacologychemistry.chemical_classificationStaining and LabelingCommunicationOrganic ChemistryDisulfide bondProteinsCombinatorial chemistryRecombinant Proteins0104 chemical sciencesAllyl CompoundsLuminescent Proteins030104 developmental biologychemistryThiolRecombinant DNASurface modificationInterleukin-2PeptidesBiotechnologydescription
The attachment of two different functionalities in a site-selective fashion represents a great challenge in protein chemistry. We report site specific dual functionalizations of peptides and proteins capitalizing on reactivity differences of cysteines in their free (thiol) and protected, oxidized (disulfide) forms. The dual functionalization of interleukin 2 and EYFP proceeded with no loss of bioactivity in a stepwise fashion applying maleimide and disulfide rebridging allyl-sulfone groups. In order to ensure broader applicability of the functionalization strategy, a novel, short peptide sequence that introduces a disulfide bridge was designed and site-selective dual labeling in the presence of biogenic groups was successfully demonstrated.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2017-12-12 | Bioconjugate Chemistry |