Abstract
Peptide methionine-tyrosine (PMY), a peptide of the neuropeptide Y (NPY) superfamily isolated from the brain and intestine of the sea lamprey, had the same maximum effect but was 11-fold less potent than pig NPY in inhibiting field-stimulated contraction of the rat vas deferens, an effect mediated through the Y2 receptor. In contrast, PMY produced a 9-fold greater maximum effect but was 3-fold less potent than pig NPY in contracting the guinea pig mesenteric artery, an effect mediated through the Y1 receptor. Molecular modelling has suggested that the conformation of PMY is appreciably different from NPY only in the β-turn region of the molecule (residues 9-14). Our data suggest, therefore, that modifications in this region of NPY may useful in the design of receptor selective analogs.