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Copper-64 radiolabelling of the C2A domain of synaptotagmin I using a functionalised bis(thiosemicarbazone): A pre- and post-labelling comparison.

Abstract：

:Dysregulation of apoptosis and necrosis is central to many diseases and non-invasive imaging of cell death is an important clinical objective to stage disease or to monitor treatment progress. The C2A domain of rat synaptotagmin I binds to phosphatidylserine (PS) exposed during cell death and modification to its lysine residues has been shown to disrupt PS binding. Site-specifically labelled (99m)Tc(CO)3-C2AcH and (68)Ga-C2Ac have previously been investigated for single photon emission computed tomography (SPECT) and positron emission tomography (PET) imaging, respectively. We wished to design a (64)Cu-labelled counterpart due to the longer half-life of (64)Cu. Since the calcium binding sites in C2A may interfere with copper binding we sought a high affinity, fast labelling chelator. We synthesised a maleimide functionalised bis(thiosemicarbazone), H2ATSE/AMal, for the site-specific copper-64 radiolabelling of thiol-functionalised C2Ac. When radiolabelling was performed by incubation of the ligand-protein conjugate (post-labelling approach), analysis of the resultant (64)CuATSE/AMal-C2Ac revealed that the C2Ac was able to compete for radiocopper with the chelator. In contrast, the pre-labelled (64)CuATSE/AMal-C2Ac conjugate revealed good stability in serum and maintained target affinity in a red blood cell binding assay. The results suggest that due to the intrinsic copper binding properties of the protein, a pre-labelling approach is preferred for the C2Ac domain of synaptotagmin I when copper is the desired radioisotope.

journal_name

J Inorg Biochem

journal_title

Journal of inorganic biochemistry

authors

Hueting R,Tavaré R,Dilworth JR,Mullen GE

doi

10.1016/j.jinorgbio.2013.07.017

subject

Has Abstract

pub_date

2013-11-01 00:00:00

pages

108-11

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(13)00172-4

journal_volume

128

pub_type

杂志文章

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