Structural investigation of Cetrorelix, a new potent and long-acting LH-RH antagonist
| Autor: | J. Engel, A. Muller, B. Kutscher, E. Busker, M. Bernd, Andrew V. Schally |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Magnetic Resonance Spectroscopy
Protein Conformation Molecular Sequence Data Antagonist Nuclear magnetic resonance spectroscopy Peptide hormone Biochemistry Mass Spectrometry Gonadotropin-Releasing Hormone chemistry.chemical_compound Protein structure chemistry Cetrorelix Solvents medicine Amino Acid Sequence Sodium dodecyl sulfate Receptor Receptors LHRH Hormone medicine.drug |
| Zdroj: | International Journal of Peptide and Protein Research. 43:264-270 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1994.tb00389.x |
| Popis: | The new decapeptide SB-75 (INN: Cetrorelix) has been characterized as a potent antagonist of luteinizing-hormone releasing hormone (LH-RH). Such derivatives are of great medicinal interest owing to their potential application in areas such as hormone-dependent tumors, uterine fibroids, and in diseases and conditions which result from inappropriate hormone levels or which can be treated by suppression of estrogens. SB-75 is the subject of intensive ongoing clinical evaluation and is an accepted standard for the design of new LH-RH antagonists. We characterized SB-75 by means of modern MS and NMR techniques to demonstrate the significance of both sequencing methods on a complicated unnatural decapeptide. Our structural elucidations with nuclear Overhauser (NOE) experiments revealed clear evidence for a highly flexible molecule with no single predominant conformation even in sodium dodecyl sulfate (SDS) mimicking a cellular membrane. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|