This review describes some of the most typical features in the evolution of neuropeptides. Neuropeptides are synthesized like other polypeptides and proteins, with an amino acid sequence determined by the DNA sequence of the corresponding gene. Mutations of bases in the coding regions of the DNA lead to changes in amino acid sequence, and explain the differences in amino acid sequence of a certain neuropeptide in different animal species. The more distantly related two species are, the more substitutions can be found in one and the same neuropeptide. The biologically active part of the neuropeptide is usually the most conserved part. Neuropeptides also form families of closely related peptides, where several members may occur in one animal species. This is due to gene or exon duplications followed by mutations. Gene splicing and posttranslational processing decides the gene product in a single cell. Difference in sequence may cause difference in function, but more often than not, members of a family appear to produce the same effect. Three neuropeptide families, the tachykinins, the neuropeptide Y family, and the vasoactive intestinal polypeptide/pituitary adenylate cyclase-activating peptide family will be described in more detail.