title: Conformation studies on bombesin receptor antagonists: 500 MHz NMR and CD characterization of synthetic (D-Phe12, Leu14)-bombesin.
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.
authors.affiliation: Institute of Industrial Chemistry, University of Padova, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Di Bello
authors.forename: A
authors.initials: A
authors.lastname: Scanelli
authors.forename: M G
authors.initials: MG
authors.lastname: Corradini
authors.forename: L
authors.initials: L
authors.lastname: Paolillo
authors.forename: E
authors.initials: E
authors.lastname: Trivellone
authors.forename: A
authors.initials: A
authors.lastname: Scatturin
authors.forename: G
authors.initials: G
authors.lastname: Vertuani
authors.forename: L
authors.initials: L
authors.lastname: Gozzini
authors.forename: R
authors.initials: R
authors.lastname: de Castiglione
mesh_terms: D001839:Bombesin / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D018004:Receptors, Bombesin; D017981:Receptors, Neurotransmitter / Q000187:drug effects / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D018004:Receptors, Bombesin; D017981:Receptors, Neurotransmitter; C051814:bombesin, Phe(12), Leu(14)-; D001839:Bombesin