Site-specific radioiodination of an anti-HER2 single domain antibody fragment with a residualizing prosthetic agent

• Published in: Nuclear medicine and biology Vol. 92; pp. 171 - 183
• Main Authors: Feng, Yutian, Zhou, Zhengyuan, McDougald, Darryl, Meshaw, Rebecca L., Vaidyanathan, Ganesan, Zalutsky, Michael R.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.01.2021; Elsevier BV
• Subjects: Affinity; Animals; Antibodies; Binding; Catabolites; Cell Line, Tumor; Coinjection; Conjugates; Conjugation; Domains; ErbB-2 protein; Female; Humans; Immunoreactivity; Internalization; Intracellular; Iodine 131; Iodine radioisotopes; Iodine Radioisotopes - chemistry; Kidneys; Labelling; Metabolites; Mice; Nanobodies; Nanobody; Ovarian cancer; Ovarian carcinoma; Pharmaceuticals; Prostheses; Radiochemistry; Radioiodination; Radioisotopes; Reagents; Receptor, ErbB-2 - immunology; Receptor, ErbB-2 - metabolism; Retention; Single domain antibody fragment; Single-Domain Antibodies - chemistry; Site-specific labeling; Tissue Distribution; Tumors; VHH; Xenografts; Xenotransplantation; Nanobody; Radioiodination; Single domain antibody fragment; Site-specific labeling; VHH

As a consequence of their small size, high stability and high affinity, single domain antibody fragments (sdAbs) are appealing targeting vectors for radiopharmaceutical development. With sdAbs binding to internalizing receptors like HER2, residualizing prosthetic agents can enhance tumor retention o...