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Positioning of Tc-99m-chelators influences radiolabeling, stability and biodistribution of Affibody molecules
KTH, School of Biotechnology (BIO).
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2009 (English)In: Bioorganic & Medicinal Chemistry Letters, ISSN 0960-894X, E-ISSN 1090-2120, 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.

Place, publisher, year, edition, pages
2009. Vol. 19, no 14, 3912-3914 p.
Keyword [en]
Affibody molecule, Tc chelator, Molecular imaging, Peptide synthesis, malignant-tumors, binding-proteins, chelators
Identifiers
URN: urn:nbn:se:kth:diva-18587DOI: 10.1016/j.bmcl.2009.03.083ISI: 000267762600051Scopus ID: 2-s2.0-67649657953OAI: oai:DiVA.org:kth-18587DiVA: diva2:336634
Note
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved

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Eriksson Karlström, Amelie

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