99mTc-labeling and in vitro characterization of N4- and N3S-RGDS-derivative peptides
| Autor: | A. Perera Pintado, M. A. Stalteri, M. Bequet Romero, S. J. Mather, O. Reyes Acosta, A. Hernández Cairo, A. Prats Capote, D. Allison |
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| Rok vydání: | 2007 |
| Předmět: |
chemistry.chemical_classification
Health Toxicology and Mutagenesis Public Health Environmental and Occupational Health Peptide Pollution High-performance liquid chromatography Blood proteins In vitro Analytical Chemistry chemistry.chemical_compound Nuclear Energy and Engineering chemistry Biochemistry Yield (chemistry) Radiology Nuclear Medicine and imaging Chelation Spectroscopy Derivative (chemistry) Cysteine |
| Zdroj: | Journal of Radioanalytical and Nuclear Chemistry. 275:619-626 |
| ISSN: | 1588-2780 0236-5731 |
| DOI: | 10.1007/s10967-007-6867-y |
| Popis: | The aim of this work was to characterize the in vitro behavior of N4- and N3S-RGDS-derivative peptides labeled with 99mTc. Peptides AGGG-Abu-GRGDSPK-NH2 (F22) and C(acm)-GGG-Abu-GRGDSPK-NH2 (SMA1) were synthesized by solid phase. The stability of 99mTc-labeled peptides was assessed in a 30-fold molar excess of cysteine and in plasma. The affinity for plasma proteins was also evaluated. Labeling yield was >95% for both peptides. 99mTc-F22 was not stable in presence of cysteine, but 63% of 99mTc remained chelated to SMA1 up to 24 hours. Both peptides showed low affinity to plasma proteins. N3S-RGDS-derivative peptide (SMA1) showed more stable coordination binding with 99mTc and a higher stability in plasma with regard to N4-RGDS-derivative peptide (F22). |
| Databáze: | OpenAIRE |
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