Comparing the measured affinity of 111In-labeled ligands for cellular receptors by monitoring gamma, beta, or X-ray radiation with three different LigandTracer® devices



LigandTracer instruments measuring high energy photons (gamma-rays), particles (electrons and positrons) and low energy photons (X-rays) are novel semi-automated devices which produce real-time radiotracer-receptor interaction data for measurement of the affinity. The affinities of two different 111In-labeled ligands were measured in three different LigandTracer devices detecting high energy gamma, Auger and internal conversion electrons, or X-rays. The obtained similar uptake/retention patterns (binding curves) show that even at low signal-to-noise ratios (data from Auger and internal conversion electrons, and X-rays), reliable binding data can be captured. This verifies that different devices could be used as alternatives for kinetic evaluation studies for radionuclides emitting different type of radiation.


111In LigandTracer Yellow LigandTracer White LigandTracer Grey Binding kinetics Affinity 



The authors thank Ridgeview Instruments AB for providing the instruments and software for this study. They also thank Assoc. Prof. Karl Anderson, Prof. Vladimir Tolmachev and Prof. Jos Buijs for their effective advice and contribution in the discussion. This work was supported by grants from Swedish Cancer Society and Swedish Research Council.


  1. 1.
    Tolmachev V, Stone-Elander S, Orlova A (2010) Current approaches to the use of radiolabeled tyrosine kinase-targeting drugs for patient stratification and treatment response monitoring: prospects and pitfalls. Lancet Oncol 11:992–10001CrossRefGoogle Scholar
  2. 2.
    Tolmachev V, Orlova A (2010) Influence of labelling methods on biodistribution and imaging properties of radiolabelled peptides for visualisation of molecular therapeutic targets. Curr Med Chem 17:2636–2655CrossRefGoogle Scholar
  3. 3.
    Fani M, Maecke HR, Okarvi SM (2012) Radiolabeled peptides: valuable tools for the detection and treatment of cancer, review. Theranostics 2(5):481–501CrossRefGoogle Scholar
  4. 4.
    Björke H, Andersson K (2006) Measuring the affinity of a radioligand with its receptor using a rotating cell dish with in situ reference area. Appl Radiat Isot 64:32–37CrossRefGoogle Scholar
  5. 5.
    Malviya G, De Vries EFJ, Dierckx RA, Signore A (2011) Synthesis and evaluation of 99mTc-labelled monoclonal antibody 1D09C3 for molecular imaging of major histocompatibility complex class II protein expression. Mol Imaging Biol 13:930–939CrossRefGoogle Scholar
  6. 6.
    Galli F, Manni I, Piaggio G et al (2014) 99mTc-Labeled-rhTSH analogue (TR1401) for imaging poorly differentiated metastatic thyroid cancer. Thyroid 24:1297–1308CrossRefGoogle Scholar
  7. 7.
    Honarvar H, Jokilaakso N, Andersson K et al (2013) Evaluation of backbone-cyclized HER2-binding 2-helix affibody molecule for in vivo molecular imaging. Nucl Med Biol 40:378–386CrossRefGoogle Scholar
  8. 8.
    Varasteh Z, Veilikyan I, Lindeberg G et al (2013) Synthesis and characterization of a high-affinity NOTA-conjugated bombesin antagonist for GRPR-targeted tumor imaging. Bioconjug Chem 24:1144–1153CrossRefGoogle Scholar
  9. 9.
    Curiotto G, Galli F, Malviya G, Signore A (2010) Use of LigandTracer for evaluating binding of radiolabelled probes to cells in suspension. Q J Nucl Med Mol Imaging 54(2):4–5Google Scholar
  10. 10.
    ENSDF Decay Data in the Medical Internal Radiation Dose (MIRD) Format for 111In. National Nuclear Data Center. Retrieved 17 October 2012Google Scholar
  11. 11.
    Tolmachev V, Varasteh Z, Honarvar H et al (2014) Imaging of platelet-derived growth factor receptor β expression in glioblastoma xenografts using affibody molecule 111In-DOTA-Z09591. J Nucl Med 55:294–300CrossRefGoogle Scholar
  12. 12.
    Jason-Moller L, Murphy M, Bruno J (2006) Overview of Biacore systems and their applications. Current Protocols in Protein Science Chapter 19: Unit 19.13Google Scholar
  13. 13.
    Björkelund H, Gedda L, Malmqvist M, Andersson K (2013) Resolving the EGF-EGFR interaction characteristics through a multiple-temperature, multiple-inhibitor, real-time interaction analysis approach. Mol Clin Oncol 1:343–352Google Scholar

Copyright information

© Akadémiai Kiadó, Budapest, Hungary 2014

Authors and Affiliations

  1. 1.Preclinical PET Platform, Department of Medicinal Chemistry, Faculty of PharmacyUppsala UniversityUppsalaSweden

Personalised recommendations