Egli, A; Alberto, R; Tannahill, L; Schibli, R; Abram, U; Schaffland, A; Waibel, R; Tourwé, D; Jeannin, L; Iterbeke, K; Schubiger, P A (1999). Organometallic 99mTc-aquaion labels peptide to an unprecedented high specific activity. Journal of Nuclear Medicine, 40(11):1913-1917.
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A new peptide labeling method that uses the organometallic aquaion [99mTc(H2O)3(CO)3]+ has been developed. METHODS: A selection of amino acids was labeled at different concentrations with the organometallic aquaion, and the labeling yield was determined by high-performance liquid chromatography. This investigation has shown histidine to be a very potent ligand, with specific activities of up to 6 TBq/micromol (160 Ci/micromol) ligand. Histidine derivatives have been coupled to neurotensin(8-13) (NT[8-13]) and have been labeled with the aquaion, resulting in high specific activities with (N(alpha)-histidinyl)acetic acid-NT(8-13) similar to those with histidine. RESULTS: Histidine derivatives of NT(8-13) labeled using this approach fully retained their receptor affinity, showing KD values of all investigated NT analogs below 1 nmol/L on colon carcinoma HT29 cells. Biodistrbution experiments in BALB/c mice showed complete clearance of (N(alpha)-histidinyl)acetic acid-NT(8-13) from the blood after 24 h and no unwanted accumulation in any tissue. CONCLUSION: The novel labeling method using the organometallic 99mTc-aquaion combines the advantage of highest specific activities with minimal functionalization of proteins and peptides under retention of biologic affinity.
|Item Type:||Journal Article, refereed|
|Communities & Collections:||07 Faculty of Science > Department of Chemistry|
|Dewey Decimal Classification:||540 Chemistry|
|Date:||1 November 1999|
|Deposited On:||11 Feb 2008 12:25|
|Last Modified:||27 Nov 2013 21:31|
|Publisher:||Society of Nuclear Medicine|
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