Co-Authors:
Nachman, R.J., Areawide Pest Management Research, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, United States
Aziz, O.B., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Davidovitch, M., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Kaczmarek, K., Areawide Pest Management Research, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, United States, Institute of Organic Chemistry, Technical University of Lodz, 90-924 Lodz, Poland
Zabrocki, J., Areawide Pest Management Research, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, United States, Institute of Organic Chemistry, Technical University of Lodz, 90-924 Lodz, Poland
Williams, H., Department of Chemistry, Texas A and M University, College Station, TX 77843, United States
Strey, A., Areawide Pest Management Research, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, United States
Altstein, M., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Abstract:
The pyrokinin/pheromone biosynthesis activating neuropeptide (PK/PBAN) family plays a significant role in the regulation of reproductive and developmental processes in a variety of insects. A transPro, type I beta-turn has been previously identified as important for the activity of PK/PBAN peptides. A PK/PBAN analog (PPK-Jo) incorporating a novel dihydroimidazole transPro mimetic motif was evaluated in four PK/PBAN bioassays (pheromonotropic, melanotropic, pupariation and hindgut myotropic). PPK-Jo proved to be a pure, selective melanotropic agonist in S. littoralis. The melanotropic receptor in S. littoralis demonstrates more tolerance to deviations from the ideal transPro structure than those of other PK/PBAN assays. The selective PK/PBAN agonist represents a new tool to better understand the endogenous mechanisms of these peptides and serves as a probe of the plasticity of PK/PBAN regulated systems and receptors. The dihydroimidazoline moiety is shown to function as a surrogate for a transPro in certain circumstances, and provides a novel scaffold with which to construct mimetic PK/PBAN analogs with enhanced selectivity and the potential to disrupt critical physiological processes in insect pests.
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