NMR Solution Structure Analysis of the C-terminal Linear and Cyclic Peptides of Pheromone Biosynthesis-Activating Neuropeptide (PBAN) from the Silkmoth Bombyx mori

摘要

In most moths, the sex pheromone production is regulated by pheromone biosynthesisactivating neuropeptide (PBAN), a 33-34 amino acid neuropeptide [1]. PBAN exerts its pheromonotropic effects by binding to PBANR, a member of G protein-coupled receptors (GPCR), predominantly expressed in the pheromone-producing cells of the female pheromone gland [2]. The shortest peptide with the pheromonotropic activity is the C-terminal pentapeptide-amide, PBAN(29-33)-NH2 (FSPRL-NH2), and the C-terminal amide group is required for the activity of PBAN [3]. In this study, we have analyzed the solution structures of the C-terminal decapeptides of PBAN with an amidated and a free C-termini (active and inactive, respectively), and an active cyclic octapeptide by two-dimensional NMR, and compared their structures to reveal the structural requirements for the PBAN activity.