Stable one-step technetium-99m labeling of His-tagged recombinant proteins with a novel Tc(I)-carbonyl complex.
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| Názov: | Stable one-step technetium-99m labeling of His-tagged recombinant proteins with a novel Tc(I)-carbonyl complex. |
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| Autori: | Waibel, R., Alberto, R., Willuda, J., Finnern, R., Schibli, R., Stichelberger, A., Egli, A., Abram, U., Mach, J.P., Plückthun, A., Schubiger, P.A. |
| Rok vydania: | 1999 |
| Zbierka: | Université de Lausanne (UNIL): Serval - Serveur académique lausannois |
| Predmety: | Aldehydes, Animals, Antibodies/genetics, Antibodies/immunology, Chromatography, Affinity, Histidine/chemistry, Humans, Immunoglobulin Fragments/chemistry, Isotope Labeling/methods, Ketones, Mice, Nude, Mucin-1/immunology, Organotechnetium Compounds/chemical synthesis, Organotechnetium Compounds/pharmacokinetics, Radiopharmaceuticals/chemical synthesis, Radiopharmaceuticals/pharmacokinetics, Recombinant Proteins/chemistry, Recombinant Proteins/pharmacokinetics, Technetium, Tissue Distribution |
| Popis: | We have developed a technetium labeling technology based on a new organometallic chemistry, which involves simple mixing of the novel reagent, a 99m Tc(I)-carbonyl compound, with a His-tagged recombinant protein. This method obviates the labeling of unpaired engineered cysteines, which frequently create problems in large-scale expression and storage of disulfide-containing proteins. In this study, we labeled antibody single-chain Fv fragments to high specific activities (90 mCi/mg), and the label was very stable to serum and all other challenges tested. The pharmacokinetic characteristics were indistinguishable from iodinated scFv fragments, and thus scFV fragments labeled by the new method will be suitable for biodistribution studies. This novel labeling method should be applicable not only to diagnostic imaging with 99mTc, but also to radioimmunotherapy approaches with 186/188 Re, and its use can be easily extended to almost any recombinant protein or synthetic peptide. |
| Druh dokumentu: | article in journal/newspaper |
| Jazyk: | English |
| ISSN: | 1087-0156 |
| Relation: | Nature Biotechnology; https://iris.unil.ch/handle/iris/197333; serval:BIB_9887E1FCA808; 000082365800033 |
| DOI: | 10.1038/12890 |
| Dostupnosť: | https://iris.unil.ch/handle/iris/197333 https://doi.org/10.1038/12890 |
| Prístupové číslo: | edsbas.238300B8 |
| Databáza: | BASE |
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Nájsť tento článok vo Web of Science | Abstrakt: | We have developed a technetium labeling technology based on a new organometallic chemistry, which involves simple mixing of the novel reagent, a 99m Tc(I)-carbonyl compound, with a His-tagged recombinant protein. This method obviates the labeling of unpaired engineered cysteines, which frequently create problems in large-scale expression and storage of disulfide-containing proteins. In this study, we labeled antibody single-chain Fv fragments to high specific activities (90 mCi/mg), and the label was very stable to serum and all other challenges tested. The pharmacokinetic characteristics were indistinguishable from iodinated scFv fragments, and thus scFV fragments labeled by the new method will be suitable for biodistribution studies. This novel labeling method should be applicable not only to diagnostic imaging with 99mTc, but also to radioimmunotherapy approaches with 186/188 Re, and its use can be easily extended to almost any recombinant protein or synthetic peptide. |
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| ISSN: | 10870156 |
| DOI: | 10.1038/12890 |