GNFFRFamide: a novel FMRFamide-immunoreactive peptide isolated from the sheep tapeworm, Moniezia expansa

The widespread distribution of FMRFamide-immunoreactivity in platyhelminth nervous systems has been demonstrated immunocytochemically. Here we report the isolation and primary structure of the first platyhelminth FMRFamide-related peptide (FaRP) from the tapeworm, Moniezia expansa. The peptide was found to have a molecular mass of 785 Da and a primary structure of Gly-Asn-Phe-Phe-Arg- Phe-NH2 (GNFFRFamide). Acid alcohol extracts of this platyhelminth contained only this single FaRP which had a phenylalanyl (F) residue in the variable position 3 from the C-terminal occupied by either methionyl (M), leucyl (L) or isoleucyl (I) residues in most other FaRPs.