{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["13(26)"],"submitter":["Rodriguez C"],"pubmed_abstract":["We report the <i>in vitro</i> characterization and <i>in vivo</i> evaluation of a novel <sup>89</sup>Zr-labeled radioimmunoconjugate synthesized using a site-selective bioconjugation strategy based on the oxidation of tyrosinase residues exposed by the deglycosylation of the IgG and the subsequent strain-promoted oxidation-controlled 1,2-quinone cycloaddition between these amino acids and <i>trans</i>-cyclooctene-bearing cargoes. More specifically, we site-selectively modified a variant of the A33 antigen-targeting antibody huA33 with the chelator desferrioxamine (DFO), thereby producing an immunoconjugate (DFO-<sup>SPOCQ</sup>huA33) with equivalent antigen binding affinity to its parent immunoglobulin but attenuated affinity for the FcγRI receptor. This construct was subsequently radiolabeled with [<sup>89</sup>Zr]Zr<sup>4+</sup> to create a radioimmunoconjugate - [<sup>89</sup>Zr]Zr-DFO-<sup>SPOCQ</sup>huA33 - in high yield and specific activity that exhibited excellent <i>in vivo</i> behavior in two murine models of human colorectal carcinoma."],"journal":["RSC advances"],"pagination":["17705-17709"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10258682"],"repository":["biostudies-literature"],"pubmed_title":["Site-selective radiolabeling using mushroom tyrosinase and the strain-promoted oxidation-controlled 1,2-quinone cycloaddition."],"pmcid":["PMC10258682"],"pubmed_authors":["Hosny MM","Thau S","Delaney S","Rodriguez C","Sarrett SM","Cornejo MA","Sebastiano J","Zeglis BM"],"additional_accession":[]},"is_claimable":false,"name":"Site-selective radiolabeling using mushroom tyrosinase and the strain-promoted oxidation-controlled 1,2-quinone cycloaddition.","description":"We report the <i>in vitro</i> characterization and <i>in vivo</i> evaluation of a novel <sup>89</sup>Zr-labeled radioimmunoconjugate synthesized using a site-selective bioconjugation strategy based on the oxidation of tyrosinase residues exposed by the deglycosylation of the IgG and the subsequent strain-promoted oxidation-controlled 1,2-quinone cycloaddition between these amino acids and <i>trans</i>-cyclooctene-bearing cargoes. More specifically, we site-selectively modified a variant of the A33 antigen-targeting antibody huA33 with the chelator desferrioxamine (DFO), thereby producing an immunoconjugate (DFO-<sup>SPOCQ</sup>huA33) with equivalent antigen binding affinity to its parent immunoglobulin but attenuated affinity for the FcγRI receptor. This construct was subsequently radiolabeled with [<sup>89</sup>Zr]Zr<sup>4+</sup> to create a radioimmunoconjugate - [<sup>89</sup>Zr]Zr-DFO-<sup>SPOCQ</sup>huA33 - in high yield and specific activity that exhibited excellent <i>in vivo</i> behavior in two murine models of human colorectal carcinoma.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2025-04-26T09:42:43.165Z","creation":"2025-04-26T09:42:43.165Z"},"accession":"S-EPMC10258682","cross_references":{"pubmed":["37313000"],"doi":["10.1039/d3ra03486k"]}}