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- W4308792209 abstract "Because of their rapid tumor accumulation and normal tissue clearance, single-domain antibody fragments (sdAbs) are an attractive vehicle for developing radiotherapeutics labeled with the α-emitter 211At. Herein, we have evaluated iso-[211At]AGMB-PODS, a prosthetic agent that combines a functionality for residualizing radiohalogens with a phenyloxadiazolyl methylsulfone (PODS) moiety for site-specific sdAb conjugation. Iso-[211At]AGMB-PODS and its radioiodinated analogue were evaluated for thiol-selective conjugation to anti-HER2 5F7 sdAb bearing a C-terminus GGC tail. Both radiohalogenated PODS-5F7GGC conjugates were synthesized in good radiochemical yields and retained high binding affinity on HER2-positive BT474 breast carcinoma cells. Iso-[211At]AGMB-PODS-5F7GGC was considerably more stable in vitro than its maleimide analogue in the presence of cysteine and human serum albumin (HSA) and exhibited excellent tumor uptake and high in vivo stability. Superior tumor-to-kidney activity ratios were seen for both radiohalogenated PODS-5F7GGC conjugates compared with [177Lu]Lu-DOTA-PODS-5F7GGC. These results suggest that iso-[211At]AGMB-PODS-5F7GGC warrants further evaluation for the treatment of HER2-expressing malignancies." @default.
- W4308792209 created "2022-11-15" @default.
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- W4308792209 date "2022-11-11" @default.
- W4308792209 modified "2023-10-16" @default.
- W4308792209 title "Site-Specific Radiohalogenation of a HER2-Targeted Single-Domain Antibody Fragment Using a Novel Residualizing Prosthetic Agent" @default.
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- W4308792209 doi "https://doi.org/10.1021/acs.jmedchem.2c01331" @default.
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