Synthesis of a tritiated human growth hormone releasing peptide
| Autor: | J. R. Heys, A. Y. L. Shu |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Indole test
chemistry.chemical_classification Magnetic Resonance Spectroscopy Molecular Structure Stereochemistry Molecular Sequence Data Peptide Tritium Cleavage (embryo) Anisole Biochemistry Hormones Hydrofluoric Acid chemistry.chemical_compound Electrophilic substitution Residue (chemistry) chemistry Peptide synthesis Humans Amino Acid Sequence Oligopeptides Peptide sequence |
| Zdroj: | International Journal of Peptide and Protein Research. 42:432-439 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1993.tb00150.x |
| Popis: | Tritium-labeled growth hormone releasing peptide His-D-Trp-Ala-Trp-D-Phe-Lys-NH2 was synthesized by tritium-halogen exchange on the precursor His-5,7-Br2-D-Trp-Ala-Trp-D-Phe-Lys-NH2. The radiolabeled peptide had a specific activity of 29 Ci/mmol and a radiochemical purity of 95%. The tritium label was shown by 3H NMR to be located mostly at the expected 5,7-positions of the indole nucleus in the D-Trp residue. The dibromopeptide was prepared by solid-phase peptide synthesis, employing racemic 5,7-Br2-Trp as a building block and separation of the resulting epimeric mixture by HPLC. 5,7-Br2-Trp was prepared by a five-step sequence beginning with 2,4-dibromoaniline. The use of anisole as an additive in the HF resin/peptide cleavage was rejected because anisole was found to undergo electrophilic substitution of the dibromoindole nucleus; a modified HF deprotection/cleavage procedure was developed and used instead. |
| Databáze: | OpenAIRE |
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