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 [H-3]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. (C) 1997 Academic Press.