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Conformation studies on bombesin receptor antagonists: 500 MHz NMR and CD characterization of synthetic (D-Phe12, Leu14)-bombesin

1989; Elsevier BV; Volume: 161; Issue: 3 Linguagem: Inglês

10.1016/0006-291x(89)91340-5

1090-2104

Carlo Di Bello, Alberto Scanelli, Maria G. Corradini, Livio Paolillo, E. Trivellone, Angelo Scatturin, Gianni Vertuani, Luigia Gozzini, Roberto Castiglione,

Receptor Mechanisms and Signaling

The conformation flexibility of the tetradecapeptide hormone bombesin and its synthetic antagonist (DPhe12, Leu14)-bombesin has been studied using nuclear magnetic resonance and circular dichroism techniques. The spectral features observed indicate that the ordered structure present in the C-terminal pentapeptide moiety of native BBS is lost in the (DPhe12, Leu14) analog.