Sex pheromone production in females of many species of moths is controlled by a pheromone biosynthesis activating neuropeptide (PBAN). PBAN from Helicoverpa zea (Hez-PBAN) is a 33 amino acid peptide produced in the suboesophageal ganglion of both female and male moths. PBAN-like activity is widespread among Lepidoptera and is also reported from a cockroach and a grasshopper. The C-terminal pentapeptide of Hez-PBAN represents the minimum sequence with pheromonotropic activity. Another pentapeptide fragment of the molecule also has high pheromonotropic activity. Presence of PBAN-like immunoreactivity and biological activity in the corpora cardiaca suggests that it is the possible site of PBAN release. There is evidence that PBAN action on pheromone gland is mediated by a second messenger. Several possible sites of action of PBAN have been suggested in the biosynthetic pathway of pheromones. The gene for Hez-PBAN has been cloned and sequenced. Cloning of a synthetic PBAN gene into a baculovirus has been attempted. Studies to isolate and identify the receptors for PBAN as well as the metabolic fate of PBAN have been initiated. © 1993 Wiley-Liss, Inc.