Conformation studies on bombesin receptor antagonists: 500 MHz NMR and CD characterization of synthetic (D-Phe12, Leu14)-bombesin.
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.
Di Bello
C
C
Institute of Industrial Chemistry, University of Padova, Italy.
Scanelli
A
A
Corradini
M G
MG
Paolillo
L
L
Trivellone
E
E
Scatturin
A
A
Vertuani
G
G
Gozzini
L
L
de Castiglione
R
R
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
D018004:Receptors, Bombesin; D017981:Receptors, Neurotransmitter; C051814:bombesin, Phe(12), Leu(14)-; D001839:Bombesin