Abstract
Bombesin (Bn, pGlu-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2) is one of the most potent peptides, possessing a variety of physiological and pharmacological functions. We find from CD spectroscopy that the eight C-terminal residues of bombesin [Bn(7-14)NH2] have an ordered structure, and replacement of His-12 with Pro of Bn(7-14)NH2 changes the conformation from ordered to a more unordered form. Antibodies to Bn(7-14)NH2 cross-react to Bn and gastrin releasing peptide (GRP) in a dose-dependent manner. Antibodies to the Pro-analog do not recognize Bn or GRP. Substitution of the C-terminal amide by isopropylamide [Bn(7-14)NHC3H7(i)] makes its antibodies more specific to Bn than to GRP. It appears that this region of the peptide is an important antigenic determinant, which makes these antibodies differentiate between BN and GRP.
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