Blower, P.J. and Surfraz, M.B. and King, R. and Biagini, S.C.G. and Mather, S.J. (2007) How do HYNIC-conjugated peptides bind technetium? Insights from LC-MS and stability studies. European Journal of Nuclear Medicine and Molecular Imaging, 34 (Sup 2). S148-S148. ISSN 1619-7070.
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| Official URL http://dx.doi.org/10.1007/s00259-007-0547-6 |
Abstract
Hydrazinonicotinamide (HYNIC) is an established bifunctional complexing agent for technetium-99m (99mTc) but the structure of the technetium coordination sphere remains uncertain. To gain further insight into this, we have prepared conjugates of HYNIC and hydrazinobenzoic acid (HYBA) with a model peptide, and radiolabelled them with 99mTc using three well-established co-ligand systems: EDDA, tricine and tricine–nicotinic acid. The labelled peptides were studied by LC-MS and by subjecting them to serum stability and protein binding assays. For each co-ligand system, HYNIC conjugates formed fewer and more stable labelled species than the corresponding HYBA conjugates. LC-MS analysis showed that all conjugates contained one hydrazine moiety bound to Tc, that binding of Tc to HYNIC–peptide and co-ligand occurs with displacement of 5H+ indicating a Tc formal oxidation state of +5, and that the Tc has no oxo- or halide ligands. LC-MS also shows that complexes formed with the HYNIC conjugate contain fewer coordinating co-ligand molecules than the HYBA conjugate indicating that HYNIC is able to more effectively satisfy the coordination requirement of technetium, perhaps by binding in chelating mode.
| Item Type: | Article |
|---|---|
| Additional information: | Abstracts of the Annual Congress of the EANM 2007, Copenhagen, Denmark |
| Subjects: | Q Science Q Science > QD Chemistry R Medicine |
| Divisions: | Faculties > Science Technology and Medical Studies > School of Physical Sciences > Functional Materials Group Faculties > Science Technology and Medical Studies > School of Physical Sciences |
| Depositing User: | Stefano C G Biagini |
| Date Deposited: | 07 Sep 2009 12:12 |
| Last Modified: | 18 Aug 2011 08:58 |
| Resource URI: | http://kar.kent.ac.uk/id/eprint/13246 (The current URI for this page, for reference purposes) |
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