ArticleEJNMMI research2014
Optimising the radiolabelling properties of technetium tricarbonyl and His-tagged proteins.
Article in EJNMMI research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
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- NOTA and NODAGA Radionuclide Complexing Agents: Versatile Approaches for Advancements in Radiochemistry.Molecules (Basel, Switzerland) · 2025Review
- Collagen Hybridizing Peptide-Based Radiotracers for Molecular Imaging of Collagen Turnover in Pulmonary Fibrosis.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2025Article
- Localized In Vivo Prodrug Activation Using Radionuclides.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2025Article
- Transplanted Murine Tumours SPECT Imaging withInternational journal of molecular sciences · 2024Article
- Tc-99m-tamoxifen: A novel diagnostic imaging agent for estrogen receptor-expressing breast cancer patients.Diagnostic and interventional radiology (Ankara, Turkey) · 2022Article
- Optimal His-Tag Design for Efficient [Bioconjugate chemistry · 2021Article
- Nanobodies asRSC chemical biology · 2021Review
- Synthesis of Radiolabeled Technetium- and Rhenium-Luteinizing Hormone-Releasing Hormone (ACS omega · 2021Article
- Preclinical development and characterisation ofAmerican journal of nuclear medicine and molecular imaging · 2021Article
- Novel Matrix Metalloproteinase 12 Selective Radiotracers for Vascular Molecular Imaging.Journal of medicinal chemistry · 2019Article
- Early Phase I Study of aJournal of nuclear medicine : official publication, Society of Nuclear Medicine · 2019Article
- Site-specific chelator-antibody conjugation for PET and SPECT imaging with radiometals.Drug discovery today. Technologies · 2018Review
- High-throughput high-volume nuclear imaging for preclinical in vivo compound screeningEJNMMI research · 2017Article
- A 99mTc-labelled scFv antibody fragment that binds to prostate-specific membrane antigen.Nuclear medicine communications · 2017Article
- Engineering hepatitis B virus core particles for targeting HER2 receptors in vitro and in vivo.Biomaterials · 2017Article
- Development ofInternational journal of nanomedicine · 2017Article
- Site-Specifically Labeled Immunoconjugates for Molecular Imaging--Part 2: Peptide Tags and Unnatural Amino Acids.Molecular imaging and biology · 2016Review
- Opportunities and challenges for metal chemistry in molecular imaging: from gamma camera imaging to PET and multimodality imaging.Advances in inorganic chemistry · 2016Article
- A nuclear chocolate box: the periodic table of nuclear medicine.Dalton transactions (Cambridge, England : 2003) · 2015Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
backgroundTo date, the majority of protein-based radiopharmaceuticals have been radiolabelled using non-site-specific conjugation methods, with little or no control to ensure retained protein function post-labelling. The incorporation of a hexahistidine sequence (His-tag) in a recombinant protein can be used to site-specifically radiolabel with 99mTc-tricarbonyl ([99mTc(CO)3]+). This chemistry has been made accessible via a technetium tricarbonyl kit; however, reports of radiolabelling efficiencies and specific activities have varied greatly from one protein to another. Here, we aim to optimise the technetium tricarbonyl radiolabelling method to produce consistently >95% radiolabelling efficiencies with high specific activities suitable for in vivo imaging.
methodsFour different recombinant His-tagged proteins (recombinant complement receptor 2 (rCR2) and three single chain antibodies, α-CD33 scFv, α-VCAM-1 scFv and α-PSMA scFv), were used to study the effect of kit volume, ionic strength, pH and temperature on radiolabelling of four proteins.
resultsWe used 260 and 350 μL [99mTc(CO)3]+ kits enabling us to radiolabel at higher [99mTc(CO)3]+ and protein concentrations in a smaller volume and thus increase the rate at which maximum labelling efficiency and specific activity were reached. We also demonstrated that increasing the ionic strength of the reaction medium by increasing [Na+] from 0.25 to 0.63 M significantly increases the rate at which all four proteins reach a >95% labelling efficiency by at least fourfold, as compared to the conventional IsoLink® kit (Covidien, Petten, The Netherlands) and 0.25 M [Na+].
conclusionWe have found optimised kit and protein radiolabelling conditions suitable for the reproducible, fast, efficient radiolabelling of proteins without the need for post-labelling purification.
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Registered trials
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