| Autor: |
J T, Elliott, W J, Hoekstra, C K, Derian, M F, Addo, B E, Maryanoff, D G, Ahern, G D, Prestwich |
| Rok vydání: |
2001 |
| Předmět: |
|
| Zdroj: |
The journal of peptide research : official journal of the American Peptide Society. 57(6) |
| ISSN: |
1397-002X |
| Popis: |
Six photoactivatable analogs of the human thrombin receptor activating peptide (TRAP), SFLLRN-NH2, were synthesized by substituting the photoactive amino acid, p-benzoylphenylalanine (Bpa), into each position of the peptide sequence. Platelet aggregation assays indicated that the peptides with Bpa substitutions at positions 3 to 6 retained agonist activity. These peptides were prepared in tritiated form as potential thrombin receptor photoaffinity labels. The [3H]Bpa-containing analogs were constructed by resynthesizing the peptides with the amino acid, 4-benzoyl-2',5'-dibromophenylalanine (Br2Bpa), and subjecting the purified peptides to Pd-catalyzed tritiodebromination. The radiochemical yields for the reductive tritiation were2% for peptides with [3H]Bpa in the third and fourth positions, and between 7 and 16% for the peptides with substitutions at the fifth and sixth positions. The low yields were due to over-reduction of the Bpa carbonyl group and nonspecific degradation during reductive tritiation. This report describes the first use of Br2Bpa for the preparation of tritiated photoactivatable peptides. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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