Chemistry:α-Endorphin

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α-Endorphin
Alpha-endorphin.svg
Alpha endorphin stick molecular model.png
Identifiers
3D model (JSmol)
ChemSpider
Properties
C77H120N18O26S
Molar mass 1745.97 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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α-Endorphin (alpha-endorphin) is an endogenous opioid peptide with a length of 16 amino acids, and the amino acid sequence: Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr.[1] With the use of mass spectrometry, Nicholas Ling was able to determine the primary sequence of a-endorphin.[2]

Relation to beta- and gamma-endorphin

Endorphins are generally known as neurotransmitters that are released when the body goes into pain.[3] The three endorphins that play a role in this response are α-endorphin, β-endorphin (beta-endorphin), and γ-endorphin (gamma-endorphin) which are all derived from the same polypeptide known as pro-opiomelanocortin.[3] Although all play roles as neurotransmitters, the specific effects of all three differ. The most studied endorphin of the three is β-endorphin. α-Endorphins are known to contain one less amino acid than γ-endorphins, differing by a single leucine amino acid at the terminal end.[4] Although this may seem minor, It allows them to have vastly different effects. Studies found that γ-endorphins and α-endorphins have opposite effects which allow them to help maintain a level of homeostasis within the brain and behavior of animals.[5] All of the specific effects on the body of α-endorphins are not yet fully studied nor fully understood by the science community. However, some studies suggest that these endorphins behave similarly to amphetamines.[6] Similarly, other studies agree that Alpha-endorphins effects are similar to psychostimulant drugs.[6]

Ranking based length, α-endorphins are the shortest with 16 amino acid residues.[3] Meanwhile, the β-endorphin has the longest chain which begins with the same 16 amino acids as α-Endorphins: Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr.[3] The same sequence is also present in γ-endorphin.[3] The beginning Tyr-Gly-Gly-Phe-Met chain is also known as the N-terminal pentapeptide opioid sequence.[3] With such configuration, endorphins act as agonists to opioid receptors in the brain.[3]

Effects on behavior

Studies have shown that α-endorphin is the strongest peptide in delaying avoidance behaviors.[7] α-Endorphin has the same C-terminal sequence of β-LPH, allowing these peptides to have a high affinity for opiate binding sites.[7] Even a slight difference in the C-terminal amino acid can have drastic effects on avoidance behavior.[7] The importance in sequencing determines the function of the endorphin.[7] When an N-terminal amino acid such as tyrosine is removed, there seems to be no significant impacts on avoidance behavior.[7] However, when there are adjustments to the C-terminal sequence, like removing β-LPH 61-65; activity of the endorphin decreases.[7]

See also

  • Endorphin
  • Amphetamines

References

  1. "Specific nonopiate receptors for beta-endorphin". Science 205 (4410): 1033–1035. September 1979. doi:10.1126/science.224457. PMID 224457. Bibcode1979Sci...205.1033H. 
  2. "The expanding significance of hypothalamic peptides, or, is endocrinology a branch of neuroendocrinology?". Recent Progress in Hormone Research. Proceedings of the 1976 Laurentian Hormone Conference (Elsevier) 33: 1–28. 1977. doi:10.1016/b978-0-12-571133-3.50008-8. ISBN 978-0-12-571133-3. PMID 20649. 
  3. 3.0 3.1 3.2 3.3 3.4 3.5 3.6 "Biochemistry, Endorphin". StatPearls. Treasure Island (FL): StatPearls Publishing. 2021. http://www.ncbi.nlm.nih.gov/books/NBK470306/. 
  4. "Behavioral effects of neuropeptides: endorphins and vasopressin". Annual Review of Physiology 44 (1): 571–582. October 1982. doi:10.1146/annurev.ph.44.030182.003035. PMID 7041806. 
  5. Endorphins and schizophrenia. Progress in Brain Research. 93. 1992. pp. 433–53. 
  6. 6.0 6.1 "Selective conversion of beta-endorphin into peptides related to gamma- and alpha-endorphin". Nature 283 (5742): 96–97. January 1980. doi:10.1038/283096a0. PMID 7350533. Bibcode1980Natur.283...96B. 
  7. 7.0 7.1 7.2 7.3 7.4 7.5 "Neuropeptides in Normal and Abnormal Behavior" (in en). Endocrinology, Neuroendocrinology, Neuropeptides. Pergamon. 1981-01-01. pp. 23–38. doi:10.1016/b978-0-08-026827-9.50006-8. ISBN 978-0-08-026827-9.