opioid peptide opioid peptide opioid peptides or opiate peptides are peptides that bind to opioid receptors in the brain; opiates and opioids mimic the effect of these peptides. such peptides may be produced by the body itself, for example endorphins. the effects of these peptides vary, but they all resemble those of opiates. brain opioid peptide systems are known to play an important role in motivation, emotion, attachment behaviour, the response to stress and pain, control of food intake, and the rewarding effects of alcohol and nicotine. vertebrate endogenous opioids neuropeptideidentifierssymbolopiods_neuropeppfampf01160interproipr006024prositepdoc00964available protein structures:pfam structures / ecod pdbrcsb pdb; pdbe; pdbjpdbsumstructure summary structural correlation between met-enkephalin, an opioid peptide, (left) and morphine, an opiate drug, (right) opioid-like peptides may also be absorbed from partially digested food (casomorphins, exorphins, and rubiscolins). opioid peptides from food typically have lengths between 4–8 amino acids. endogenous opioids are generally much longer. opioid peptides are released by post-translational proteolytic cleavage of precursor proteins. the precursors consist of the following components: a signal sequence that precedes a conserved region of about 50 residues; a variable-length region; and the sequence of the neuropeptides themselves. sequence analysis reveals that the conserved n-terminal region of the precursors contains 6 cysteines, which are probably involved in disulfide bond formation. it is speculated that this region might be important for neuropeptide processing. endogenous the human genome contains several homologous genes that are known to code for endogenous opioid peptides. the nucleotide sequence of the human gene for proopiomelanocortin (pomc) was characterized in 1980. the pomc gene codes for endogenous opioids such as β-endorphin and γ-endorphin. the human gene for the enkephalins was isolated and its sequence described in 1982. the human gene for dynorphins (originally called the "enkephalin b" gene because of sequence similarity to the enkephalin gene) was isolated and its sequence described in 1983. the pnoc gene encoding prepronociceptin, which is cleaved into nociceptin and potentially two additional neuropeptides. adrenorphin, amidorphin, and leumorphin were discovered in the 1980s. the endomorphins were discovered in the 1990s. opiorphin and spinorphin, enkephalinase inhibitors (i.e., prevent the metabolism of enkephalins). hemorphins, hemoglobin-derived opioid peptides, including hemorphin-4, valorphin, and spinorphin, among others. while not peptides, codeine and morphine are also produced in the human body. endogenous opioid peptides and their receptors opioid peptide amino acid sequence opioid receptor target(s)