RESUMEN

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.

Asunto(s)

Bombesina , Bombesina/análogos & derivados , Bombesina/metabolismo , Bombesina/farmacología , Dicroismo Circular , Espectroscopía de Resonancia Magnética , Conformación Proteica , Receptores de Bombesina , Receptores de Neurotransmisores/efectos de los fármacos , Receptores de Neurotransmisores/metabolismo , Relación Estructura-Actividad