2019
DOI: 10.1007/s10989-019-09813-7
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Opioid Peptides: An Overview of Functional Significance

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Cited by 32 publications
(15 citation statements)
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“…All are produced in the hypothalamus, pituitary gland, and in different parts of the nervous system and brain. Among all of them, β-endorphins are the most powerful one and play a crucial role as a neuromodulator [ 55 ]; they help to alleviate stress, body pain, and anxiety behaviors [ 55 , 56 ]. Endomorphins consist of types 1 and 2 endomorphins and dynorphins; both are located in the central nervous system and play significant roles in pain and stress-related conditions.…”
Section: Classification Of Opioid Peptidesmentioning
confidence: 99%
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“…All are produced in the hypothalamus, pituitary gland, and in different parts of the nervous system and brain. Among all of them, β-endorphins are the most powerful one and play a crucial role as a neuromodulator [ 55 ]; they help to alleviate stress, body pain, and anxiety behaviors [ 55 , 56 ]. Endomorphins consist of types 1 and 2 endomorphins and dynorphins; both are located in the central nervous system and play significant roles in pain and stress-related conditions.…”
Section: Classification Of Opioid Peptidesmentioning
confidence: 99%
“…Furthermore, there are various other food sources too that are reported as a source of exogenous opioid peptides such as barley (hordein peptide [ 79 ]), wheat (Gluten (gluten exorphins), a major wheat protein complex, Gliadin (gliadorphin), Glutenin (gluten morphin) peptides [ 55 ]), while gliadorphin-7 (Tyr-Pro-Gln-Pro-Gln-Pro-Phe) derived from α-gliadin has shown opioid activity [ 92 ]. In another study, whey protein consisting of β-lactoglobulin, immunoglobulins, α-lactalbumin, lactoperoxidase, lactoferrin, etc.…”
Section: Classification Of Opioid Peptidesmentioning
confidence: 99%
“…Endogenous opioid peptides include endorphins, enkephalins, and dynorphins, which are produced naturally in the body from larger proteins, namely, proopiomelanocortin, proenkephalin, and prodynorphin, respectively, by enzymatic hydrolysis caused by peptidases (Pihlanto‐Leppälä, 2000). It was found that opioid peptides typically contain four to eight amino acids and share a common structural motif where they have the same N‐terminal sequence, YGGF, and are termed as typical opioid peptides (Kaur et al., 2019; Pihlanto‐Leppälä, 2000). Efforts have been made to modify these endogenous peptides into semisynthetic analogues through amino acid substitution, addition, deletion, cyclization, or hybridization to make them more potent to be used as clinical analgesics (Garg et al., 2016; Janecka et al., 2004; Liu & Wang, 2012).…”
Section: Structure–activity Relationship Of Bpsmentioning
confidence: 99%
“…Endorphins, enkephalins, dynorphins, and nociceptins/orphanins represent the four families of endogenous opioids [ 22 , 23 ]. They are peptides of varying length and are mainly synthesized and released by well-identified neuronal sub-populations located in the CNS [ 23 ]. In addition to this neuronal production, opioids can also be synthesized and released by immune cells [ 24 ].…”
Section: Opioids Immune System and Tissue Regenerationmentioning
confidence: 99%
“…They are currently called MORs, delta opioid receptors, kappa opioid receptor, and opioid-receptor-like 1 receptors. Their endogenous ligands are β-endorphin, dynorphin, met-enkephalin, and nociceptin, respectively, although these peptides show significant cross-affinity for all opioid receptors [ 22 , 23 , 26 , 27 ]. All these receptors belong to the super family of 7-domain transmembrane receptors and are predominantly coupled to G proteins of the α i or α 0 type.…”
Section: Opioids Immune System and Tissue Regenerationmentioning
confidence: 99%