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

C Di Bello; A Scanelli; M G Corradini; L Paolillo; E Trivellone; A Scatturin; G Vertuani; L Gozzini; R de Castiglione

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

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.

Authors

C Di Bello¹, A Scanelli, M G Corradini, L Paolillo, E Trivellone, A Scatturin, G Vertuani, L Gozzini, R de Castiglione

Affiliation

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bombesin* / analogs & derivatives*
Bombesin* / metabolism
Bombesin* / pharmacology
Circular Dichroism
Magnetic Resonance Spectroscopy
Protein Conformation
Receptors, Bombesin
Receptors, Neurotransmitter / drug effects
Receptors, Neurotransmitter / metabolism
Structure-Activity Relationship

Substances

Receptors, Bombesin
Receptors, Neurotransmitter
bombesin, Phe(12), Leu(14)-
Bombesin