This report summarizes recent work on the chemistry and structure-activity relationships of crustacean chromatophorotropic pigment-dispersing hormones (PDHs) and the identification of structurally related peptides from insects. So far, the primary structures of crustacean alpha-PDH and beta-PDH and of a pigment-dispersing factor (PDF) from the grasshopper Romalea microptera have been deduced. Additionally, 17 of the 18 residues of a PDF from the cricket Acheta domesticus were identified. In the PDH/PDF family, the chain length (18 residues), terminal residues (N-terminal Asn and C-terminal Ala-NH2), and at least 50% of the amino acid sequence appear to be conserved. The functions of these peptides in insects are unknown. Detailed studies of structure-activity relationships of crustacean PDHs have been conducted, leading to the tentative identification of the message sequence, preparation of hyperpotent oxidation-resistant analogs, and synthesis of bioactive tyrosinated analogs for radioiodination. Antisera were raised against PDHs, and immunoreactive soma and fibers have been localized in the crustacean eyestalk neurosecretory system. This progress is expected to stimulate more intensive research on the PDH family.