Amino acid sequence pattern in the regulatory peptides.

The essential properties of the primary structure of regulatory peptides, i.e. amino acid residues and their combinations, which are characteristic of the whole population of regulatory peptides, have been revealed using statistical methodology. These properties are as follows: increased content of certain residues (Gly, Pro, Phe, Arg, Tyr, Met and Trp) as well as an increased rate of occurrence of certain pairs of residue as compared with proteins, a random sequence of residues and "nonregulatory" peptides. By representing regulatory peptides as a sequence of hydrophobic (2 types) and hydrophilic (3 types) segments, the pattern for alternation of these segments in regulatory peptides has been determined. The segments were classified into 5 types according to the peculiarities of mutual localization of hydrophobic and hydrophilic residues within the primary structure of regulatory peptides. As compared with proteins, "nonregulatory" peptides and a random sequence of segments, regulatory peptides were characterized by an increased frequency of 4 particular pairs of segments among 12 theoretically possible pairs. These 4 pairs are fragments of the periodic segment sequence with periods of 4 segments. The revealed pattern indicates that there exists a general principle of the regulatory peptide primary structure organization and possibly a common type of the regulatory peptides flexible peptide chain folding at the ligand-receptor complex formation.

Sequence similarity between opioid peptide precursors and DNA-binding proteins.

The opioid peptide precursors, preprodynorphin and preproenkephalin show structure similarity with a transcription factor, hunchback and the putative helix-loop-helix DNA-binding proteins, lil-1, tal and twist. Segments with similarity contain the three enkephalin sequences in preprodynorphin and one in preproenkephalin which are present within heptapeptide repeats characteristic of an alpha-helical coiled-coil structure distinctive of an amphipathic helix-loop-helix DNA-binding motif. Hunchback and the opioid prohormones also have cystein-rich regions characteristic of zinc-finger domains in common.