| Autor: |
G. Van Binst, C. Wynants, H.R. Loosli |
| Rok vydání: |
2009 |
| Předmět: |
|
| Zdroj: |
International Journal of Peptide and Protein Research. 25:622-627 |
| ISSN: |
0367-8377 |
| Popis: |
The conformational properties of the somatostatin analogue 201-456 (1) have been studied by high field n.m.r. in DMSO. This analogue is the base structure of nine derivates synthesized by Bauer et al. and shows a very low biological activity, although derived structures such as SMS 201-995 (2) are very potent. Our study has shown an important difference between the most stable conformation of the two compounds: although the beta turn type II' structure at the Phe3-Trp4-Lys5 level is present in both analogues, an important conformational change appears at the cystine bridge. In SMS 201-995 the beta turn/beta sheet conformation is stabilized by the additional amino-acids D-Phe1 and Thr8 (ol) through intramolecular H-bonds. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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