Identification of soluble binding proteins for an insect neuropeptide

A photoaffinity analog of Helicoverpa zea pheromone biosynthesis activating neuropeptide (Hez-PBAN) was used to identify PBAN binding proteins in various tissues of the corn earworm moth, H. zea. Synthetic Hez-PBAN was derivatized on Lys-27 with p-benzoyldihydrocinnamoyl-N-hydroxysuccinimide ester (BZDC-NHS ester). The resulting BZDC-PBAN stimulated pheromone production in H. zea isolated abdomens at levels comparable to those of the unmodified peptide. Photoaffinity labeling experiments using [3H]BZDC-PBAN with female moth tissues revealed soluble 100 and 115 kDa proteins in the brain-subesophageal ganglia complex, ventral nerve cord, and thoracic muscle that were specifically labeled with the PBAN analog.