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Short-lived, radioactive lanthanides are attractive radioisotopes for targeted radionuclide therapy, which is a rapidly growing class of cancer treatment. To deliver such isotopes to the target cancer cells, they must be appended, i.e. chelated, to carriers that target antigens overexpressed on the target cancer cell's surface. For the production of such radiopharmaceuticals, it is highly desirable to use chelating molecules that can capture large radioisotopes with high specificity and stability under mild temperature and pH conditions, leaving the carrier protein molecule and target binding capacity intact. Here, we aim to improve the development of radiopharmaceuticlas via implementing and benchmarking protein-based alternatives to the currently used synthetic chemical chelators. As additional innovation, these protein-based alternatives will be directly fused to proteinous carriers (e.g. peptides or nanobodies), produced recombinantly and benchmarked. Both innovative approaches provide unique possibilities for targeted radionuclide therapy.