Chemistry:Hemorphin-4

From HandWiki

Hemorphin-4 is an endogenous opioid peptide of the hemorphin family which possesses antinociceptive properties and is derived from the β-chain of hemoglobin in the bloodstream.[1][2] It contains a tetrapeptide core with the amino acid sequence Tyr-Pro-Trp-Thr. Hemorphin-4 serves as a opioid receptor ligand that has affinities for the μ-, δ-, and κ-opioid receptors in the same range as the structurally related β-casomorphins, although affinity to the κ-opioid receptor is markedly higher in comparison.[3] It acts as an agonist at these sites.[4] It presents high affinity for other receptors such as angiotensin IV, bombesin subtype 3 (hBRS-3), and the corticotropin releasing factor (CRF).[5] Even though it exhibits lower binding affinity for opioid receptors relative to traditional opioid peptides such as endorphins and enkephalins; it may still influence opioid receptor systems due to its high tissue concentration.

Therapeutic potentials

Hemorphin-4 also has inhibitory effects on angiotensin-converting enzyme (ACE),[6] and as a result, may play a role in the regulation of blood pressure.[3] Notably, inhibition of ACE also reduces enkephalin catabolism.[7] Upon modifications with adamantane and cyclohexane, the Hemorphin-4 analog inhibits insulin-regulated aminopeptidase (IRAP) compared to other angiotensin IV inhibitors, making it a suitable candidate for pain, anxiety, and depression therapies.[5] In binding to the μ-opioid receptor, it has significant seizure-suppressing and pain-relieving properties and reduces involuntary bladder contractions in a similar manner to classic opioids.[8]

See also

References

  1. ↑ "Novel opioid peptides derived from hemoglobin: hemorphins". European Journal of Pharmacology 125 (2): 309–10. June 1986. doi:10.1016/0014-2999(86)90044-0. PMID 3743640. 
  2. ↑ "Peptide fragments derived from the beta-chain of hemoglobin (hemorphins) are centrally active in vivo". Peptides 10 (4): 747–51. 1989. doi:10.1016/0196-9781(89)90107-1. PMID 2587417. 
  3. ↑ 3.0 3.1 "Opioid receptor affinities of the blood-derived tetrapeptides hemorphin and cytochrophin". European Journal of Pharmacology 166 (3): 523–6. August 1989. doi:10.1016/0014-2999(89)90368-3. PMID 2553436. 
  4. ↑ "Isolation of a novel tetrapeptide with opiate and antiopiate activity from human brain cortex: Tyr-Pro-Trp-Gly-NH2 (Tyr-W-MIF-1)". Peptides 13 (4): 623–31. 1992. doi:10.1016/0196-9781(92)90165-Y. PMID 1359507. 
  5. ↑ 5.0 5.1 Mielczarek, Przemyslaw; Hartman, Kinga; Drabik, Anna; Hung, Hao-Yuan; Huang, Eagle Yi-Kung; Gibula-Tarlowska, Ewa; Kotlinska, Jolanta H.; Silberring, Jerzy (2021-06-25). "Hemorphins—From Discovery to Functions and Pharmacology" (in en). Molecules 26 (13): 3879. doi:10.3390/molecules26133879. ISSN 1420-3049. PMID 34201982. 
  6. ↑ "Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity". FEBS Letters 287 (1–2): 39–41. August 1991. doi:10.1016/0014-5793(91)80011-Q. PMID 1652464. Bibcode: 1991FEBSL.287...39L. 
  7. ↑ "Separate metabolic pathways for Leu-enkephalin and Met-enkephalin-Arg(6)-Phe(7) degradation by rat striatal synaptosomal membranes". Neurochemistry International 4 (5): 389–96. 1982. doi:10.1016/0197-0186(82)90081-X. PMID 20487892. 
  8. ↑ Ali, Amanat; Alzeyoudi, Seham Abdullah Rashed; Almutawa, Shamma Abdulla; Alnajjar, Alya Nasir; Vijayan, Ranjit (2020-08-01). "Molecular basis of the therapeutic properties of hemorphins". Pharmacological Research 158. doi:10.1016/j.phrs.2020.104855. ISSN 1043-6618. PMID 32438036. https://linkinghub.elsevier.com/retrieve/pii/S1043661820311634. 




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