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Endomorphin-2 (EM-2) is an endogenous opioid peptide and one of the two endomorphins. [1] It has the amino acid sequence Tyr-Pro-Phe-Phe-NH 2.It is a high affinity, highly selective agonist of the μ-opioid receptor, and along with endomorphin-1 (EM-1), has been proposed to be the actual endogenous ligand of this receptor (that is, rather than the endorphins).
Alternately, endomorphin-2 is predominantly found in the spinal cord, specifically in presynaptic terminals of afferent neurons in the dorsal horn region. It has been found co-localized with calcitonin as well as the pain-conveying neurotransmitter, substance P. Neither endomorphin-1 or 2 have been identified in the amygdala or the hippocampus. [2]
[12] α-endorphin and γ-endorphin result from proteolytic cleavage of β-endorphin between the Thr(16)-Leu(17) residues and Leu(17)-Phe(18) respectively. [24] α-endorphin has the shortest sequence, and β-endorphin has the longest sequence. α-endorphin and γ-endorphin are primarily found in the anterior and intermediate pituitary. [25]
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In a 1996 study, 250 to 1000 μg Semax improved attention and short-term memory in 11 healthy subjects performing 8 hour work shifts, though the effects were most pronounced when subjects were fatigued (after the shift was over) and the effects lasted going into the next day. [14]
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There are three well-characterized families of opioid peptides produced by the body: enkephalins, β-endorphin, and dynorphins.The met-enkephalin peptide sequence is coded for by the enkephalin gene; the leu-enkephalin peptide sequence is coded for by both the enkephalin gene and the dynorphin gene. [3]
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