Amidorphin
Amidorphin is a naturally occurring, endogenous peptide that is derived from proopiomelanocortin (POMC). It is a potent opioid peptide and has been found in the pituitary gland and adrenal gland of various species, including humans. Amidorphin is a heptapeptide, meaning it is composed of seven amino acids. Its sequence is Tyr-Gly-Gly-Phe-Met-Arg-Phe.
Structure and Function[edit | edit source]
Amidorphin is a heptapeptide, which means it is composed of seven amino acids. The specific sequence of amino acids in amidorphin is Tyrosine (Tyr), Glycine (Gly), Glycine (Gly), Phenylalanine (Phe), Methionine (Met), Arginine (Arg), and Phenylalanine (Phe). This sequence is often abbreviated as Tyr-Gly-Gly-Phe-Met-Arg-Phe.
Amidorphin functions as an opioid peptide, which means it binds to opioid receptors in the brain and other tissues. This binding can produce a variety of effects, including pain relief, sedation, and euphoria. Amidorphin is considered a potent opioid peptide due to its high affinity for the mu-opioid receptor, the primary target of most opioid drugs.
Biosynthesis[edit | edit source]
Amidorphin is derived from the larger protein proopiomelanocortin (POMC). POMC is a precursor protein that is cleaved by enzymes to produce several different peptides, including amidorphin. The specific enzyme responsible for the cleavage of POMC to produce amidorphin is called prohormone convertase 2 (PC2).
Distribution[edit | edit source]
Amidorphin has been found in various tissues throughout the body, including the pituitary gland and adrenal gland. It has also been detected in the brain, where it is thought to play a role in pain perception and response.
Research and Clinical Significance[edit | edit source]
Research into amidorphin and other opioid peptides may lead to new treatments for pain, addiction, and other conditions. Because amidorphin is a natural, endogenous substance, it may have fewer side effects than synthetic opioid drugs. However, more research is needed to fully understand the role of amidorphin in the body and its potential therapeutic uses.
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Contributors: Prab R. Tumpati, MD