par Jaspers, Hendrika;HORVÁTH, Anikó;MEZÖ, Imre;Kéri, György;Van Binst, Georges 
Référence International Journal of Peptide and Protein Research, 43, 3, page (271-276)
Publication Publié, 1994

Référence International Journal of Peptide and Protein Research, 43, 3, page (271-276)
Publication Publié, 1994
Article révisé par les pairs
Résumé : | A series of somatostatin analogues with varying activities have been studied by 1H NMR in CD3OH at low temperature in order to find a possible structural explanation for the differentiation of biological activities. In somatostatin analogues with GH release inhibitory activity a β‐turn/β‐sheet backbone conformation is present, which is shown to be characteristic of somatostatin‐derived peptides exhibiting this biological activity. On the other hand, among the analogues with antitumor activity, a deviation from these typical structural features is clearly observed, but no general conformational model can be proposed. Copyright © 1994, Wiley Blackwell. All rights reserved |