Contrast Agents III by Krause W.

By Krause W.

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Octreotide was labelled at the N-terminus with CpTc(CO)3 by the double ligand transfer approach in an overall 8% yield and the biodistribution was tested in rats. e. could be blocked by cold unlabelled octreotide. The compound possessed the important features of a radiopharmaceutical, in vivo stability, specific uptake and retention in target tissue and low accumulation in nontarget tissue such as fat and muscles. Still, the synthesis is not convenient and needs improvement [85]. In another approach, somatostatin 14-dextran was oxidized and coupled to histidine through imination.

Accumulation in bombesin receptor containing organs was demonstrated in tumour-bearing mice models. Since the chela- 38 R. Alberto tor is only bidentate, the third position was subsequently coordinated to the highly hydrophilic phosphine P(CH2–OH)3. This further coordination can be described as a mixed-ligand approach and resulted in significantly higher hydrophilicity of the radioconjugate and an improved biodistribution [116]. A similar investigation has also been performed with the fac-[188Re(CO)3]+ moiety [117].

A similar investigation has also been performed with the fac-[188Re(CO)3]+ moiety [117]. Beside these well known peptides, neuropeptide Y analogues have been labelled with the fac-[99mTc(CO)3]+ moiety. 2-Picolylamine-N,N-diacetic acid was coupled to the N-terminus of neuropeptide Y. The biological stability was excellent and neither cysteine nor histidine challenge replaced the label. However, since neuropeptide Y comprises a histidine in the chain, some unspecific labelling at the imidazole side chain occurred.

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