{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12(26)"],"submitter":["Rudd SE"],"funding":["Australian Cancer Research Foundation","National Health and Medical Research Council","Australian Research Council"],"pubmed_abstract":["Identification of tumors which over-express Epidermal Growth Factor Receptor (EGFR) is important in selecting patients for anti-EGFR therapies. Enzymatic bioconjugation was used to introduce positron-emitting radionuclides (<sup>89</sup>Zr, <sup>64</sup>Cu) into an anti-EGFR antibody fragment for Positron Emission Tomography (PET) imaging the same day as injection. A monovalent antibody fragment with high affinity for EGFR was engineered to include a sequence that is recognized by the transpeptidase sortase A. Two different metal chelators, one for <sup>89</sup>Zr<sup>IV</sup> and one for <sup>64</sup>Cu<sup>II</sup>, were modified with a N-terminal glycine to enable them to act as substrates in sortase A mediated bioconjugation to the antibody fragment. Both fragments provided high-qualit"],"journal":["Chemical science"],"pagination":["9004-9016"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8261882"],"repository":["biostudies-literature"],"pubmed_title":["Enzyme mediated incorporation of zirconium-89 or copper-64 into a fragment antibody for same day imaging of epidermal growth factor receptor."],"pmcid":["PMC8261882"],"pubmed_authors":["Pearce LA","Cullinane C","Hicks RJ","Raicevic A","Rudd SE","Van Zuylekom JK","Adams TE","Donnelly PS","Williams CC"],"additional_accession":[]},"is_claimable":false,"name":"Enzyme mediated incorporation of zirconium-89 or copper-64 into a fragment antibody for same day imaging of epidermal growth factor receptor.","description":"Identification of tumors which over-express Epidermal Growth Factor Receptor (EGFR) is important in selecting patients for anti-EGFR therapies. Enzymatic bioconjugation was used to introduce positron-emitting radionuclides (<sup>89</sup>Zr, <sup>64</sup>Cu) into an anti-EGFR antibody fragment for Positron Emission Tomography (PET) imaging the same day as injection. A monovalent antibody fragment with high affinity for EGFR was engineered to include a sequence that is recognized by the transpeptidase sortase A. Two different metal chelators, one for <sup>89</sup>Zr<sup>IV</sup> and one for <sup>64</sup>Cu<sup>II</sup>, were modified with a N-terminal glycine to enable them to act as substrates in sortase A mediated bioconjugation to the antibody fragment. Both fragments provided high-qualit","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jul","modification":"2026-06-02T12:30:06.608Z","creation":"2022-02-10T20:31:44.061Z"},"accession":"S-EPMC8261882","cross_references":{"pubmed":["34276928"],"doi":["10.1039/d1sc01422f"]}}