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Structural correlation between met-enkephalin, an opioid peptide (left), and morphine, an opiate drug (right) 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 ...
Activation of the μ-opioid receptor by an agonist such as morphine causes analgesia, sedation, slightly reduced blood pressure, itching, nausea, euphoria, decreased respiration, miosis (constricted pupils), and decreased bowel motility often leading to constipation. Some of these effects, such as analgesia, sedation, euphoria, itching and ...
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]
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).
Endorphins may contribute to the positive effect of exercise on anxiety and depression. [43] The same phenomenon may also play a role in exercise addiction . Regular intense exercise may cause the brain to downregulate the production of endorphins in periods of rest to maintain homeostasis , causing a person to exercise more intensely in order ...
Heterotrimeric G proteins act as ‘molecular switches’, which play a key role in signal transduction, because they relay information from activated receptors to appropriate effector proteins. All G protein α sub-units contain palmitate, which is a 16-carbon saturated fatty acid, that is attached near the N-terminus through a labile ...
The structure of morphine is not particularly complex, however the electrostatic polarization of adjacent bonded atoms does not alternate uniformly throughout the structure. This "dissonant connectivity" makes bond formation more difficult and therefore significantly complicates any synthetic strategy that is applied to this family of molecules.
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]