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

  • Biochem Biophys Res Commun. 1989 Jun 30;161(3):987-93. doi: 10.1016/0006-291x(89)91340-5.
C Di Bello  1 ,  A Scanelli ,  M G Corradini ,  L Paolillo ,  E Trivellone ,  A Scatturin ,  G Vertuani ,  L Gozzini ,  R de Castiglione
Affiliations
  • 1. Institute of Industrial Chemistry, University of Padova, Italy.
PMID: 2545203 DOI: 10.1016/0006-291x(89)91340-5
Abstract

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.

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