Chemical studies of pheromone receptors in insects
1993
Prestwich, G.D.
In the current molecular model for insect olfaction, pheromones are recognized in a minimum-energy conformation by specific receptor proteins in a dendritic membrane following their binding-protein-mediated transit through the extracellular sensory lymph. Binding to the receptor protein then triggers a G-proteinlinked phospholipase C, which releases a short pulse of the second messenger inositol 1,4,5-trisphosphate (IP3). IP3 may act via its receptor to mobilize Ca++ ions, eventually leading to a transmembrane ion current; alternatively, IP3 may directly gate the ion channel. To understand this process, we have synthesized photoaffinity labels for the pheromone receptor sites and for the IP3 receptor sites. The latter probe, [125I]-ASA-IP3, is now being employed in joint projects to identify membrane IP3 receptors in the rat brain, locust brain, rat olfactory cilia, catfish olfactory cilia, and in cockroach and moth sensilia. Fluorine-substituted pheromone analogs have also been synthesized as probes of receptor site hydrophobicity. The rationale for this approach is presented, and biological studies with selectively-fluorinated analogs of (Z)-5-decenyl acetate (Z5-10:Ac), (Z)-7-dodecenyl acetate (Z7-12:Ac), (Z)-9-dodecenyl acetate (Z9-12:Ac), (Z)-9-tetradecenyl acetate (Z9-14:Ac), (Z)-11-hexadecenal (Zll-16:Al), and several functional group derivatives for a number of economically important moth species are described.
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