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Positioning of Tc-99m-chelators influences radiolabeling, stability and biodistribution of Affibody molecules
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Oncology, Radiology and Clinical Immunology, Biomedical Radiation Sciences.ORCID iD: 0000-0001-6120-2683
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2009 (English)In: Bioorganic & Medicinal Chemistry Letters, ISSN 0960-894X, E-ISSN 1464-3405, Vol. 19, no 14, 3912-3914 p.Article in journal (Refereed) Published
Abstract [en]

Affibody molecules represent a novel class of affinity proteins with a high potential as tracers for radio-nuclide molecular imaging. In this comparative structure-property study, a series of Affibody molecules with the Tc-99m-chelators maGGG, maSSS, or maESE attached to the e-amine of the internally positioned K49 was prepared by peptide synthesis, for comparison to molecules with similar chelators positioned at the N-terminus. The conjugates were labeled with Tc-99m and evaluated in vitro and in vivo. It was found that both composition and position of the chelating moiety influence the label stability, biodistribution and targeting properties of HER2-binding Affibody molecules. (C) 2009 Elsevier Ltd. All rights reserved.

Place, publisher, year, edition, pages
2009. Vol. 19, no 14, 3912-3914 p.
Keyword [en]
Affibody molecule, Tc chelator, Molecular imaging, Peptide synthesis
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-128387DOI: 10.1016/j.bmcl.2009.03.083ISI: 000267762600051OAI: oai:DiVA.org:uu-128387DiVA: diva2:331513
Available from: 2010-07-23 Created: 2010-07-20 Last updated: 2015-03-24Bibliographically approved

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Orlova, AnnaTolmachev, Vladimir
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Biomedical Radiation SciencesDepartment of Medical Sciences
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