Studies on the Structure-Activity Relationship of Pheromone Biosynthesis-Activating Neuropeptide (PBAN)

摘要

We examined the effect of the amino acid residue at the sixth position from the C-terminus of pheromone biosynthesis-activating neuropeptide (PBAN), referred to as position C6 in this report, on the PBAN activity. We synthesized a series of PBAN analogues containing the C-terminal active core, and measured their agonistic activity by an in vitro assay system using Sf9 cells. The results showed that the PBAN analogues whose amino acid at C6 (Tyr in wild-type peptide)was replaced by Ala, Asn, Arg, Cys, Leu, Phe and Trp exhibited lower activity, and that the PBAN analogues with Ala, Asn and Leu at C6 partially inhibited the agonistic activity of the wild-type peptide.