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| Name = α-Endorphin |
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|ImageFile=alpha-endorphin.svg |
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| ImageFile2=File:Alpha endorphin stick molecular model.png |
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|Section1={{Chembox Identifiers |
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| CASNo=61512-76-3 |
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| PubChem=16138308 |
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| SMILES=C((C(=O)N(CO)C(=O)N(CCC(=O)O)C(=O)N(CCCCN)C(=O)N(CO)C(=O)N(CCC(=O)N)C(=O)N((C)O)C(=O)N1CCC1C(=O)N(CC(C)C)C(=O)N(C(C)C)C(=O)N((C)O)C(=O)O)NC(=O)(CCSC)NC(=O)(CC2=CC=CC=C2)NC(=O)CNC(=O)CNC(=O)(CC3=CC=C(C=C3)O)N)O |
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| C=77|H=120|N=18|O=26|S=1 |
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| C=77 | H=120 | N=18 | O=26 | S=1 |
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'''Alpha-endorphin''' is an ] ] whose amino acid sequence is: ]-]-Gly-]-]-]-]-]-]-Ser-]-Thr-Pro-]-]-Thr. |
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'''α-Endorphin''' (''alpha''-endorphin) is an ] ] with a length of 16 ]s, and the ]: ]-]-Gly-]-]-]-]-]-]-Ser-]-Thr-]-]-]-Thr.<ref>{{cite journal | vauthors = Hazum E, Chang KJ, Cuatrecasas P | title = Specific nonopiate receptors for beta-endorphin | journal = Science | volume = 205 | issue = 4410 | pages = 1033–1035 | date = September 1979 | pmid = 224457 | doi = 10.1126/science.224457 | bibcode = 1979Sci...205.1033H }}</ref> With the use of mass spectrometry, Nicholas Ling was able to determine the primary sequence of a-endorphin.<ref>{{cite journal | vauthors = Guillemin R | title = The expanding significance of hypothalamic peptides, or, is endocrinology a branch of neuroendocrinology? | journal = Recent Progress in Hormone Research | volume = 33 | pages = 1–28 | date = 1977 | pmid = 20649 | doi = 10.1016/b978-0-12-571133-3.50008-8 | publisher = Elsevier | isbn = 978-0-12-571133-3 | series = Proceedings of the 1976 Laurentian Hormone Conference }}</ref> |
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== Relation to beta- and gamma-endorphin == |
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{{Neuropeptides}} |
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] are generally known as ]s that are released when the body goes into ].<ref name=":0" /> The three endorphins that play a role in this response are α-endorphin, ] (''beta''-endorphin), and ] (''gamma''-endorphin) which are all derived from the same ] known as ].<ref name=":0" /> 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 ] amino acid at the terminal end.<ref>{{cite journal | vauthors = Koob GF, Bloom FE | title = Behavioral effects of neuropeptides: endorphins and vasopressin | journal = Annual Review of Physiology | volume = 44 | issue = 1 | pages = 571–582 | date = October 1982 | pmid = 7041806 | doi = 10.1146/annurev.ph.44.030182.003035 }}</ref> 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 ] within the ] and ].<ref name="pmid1480761">{{cite book | vauthors = Wiegant VM, Ronken E, Kovács G, De Wied D | title = Endorphins and schizophrenia | series = Progress in Brain Research | volume = 93 | pages = 433–53 | date = 1992 | pmid = 1480761 | doi = | url = }}</ref> 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 ].<ref name=":2">{{cite journal | vauthors = Burbach JP, Loeber JG, Verhoef J, Wiegant VM, de Kloet ER, de Wied D | title = Selective conversion of beta-endorphin into peptides related to gamma- and alpha-endorphin | journal = Nature | volume = 283 | issue = 5742 | pages = 96–97 | date = January 1980 | pmid = 7350533 | doi = 10.1038/283096a0 | bibcode = 1980Natur.283...96B | s2cid = 4340549 }}</ref> Similarly, other studies agree that Alpha-endorphins effects are similar to ]s.<ref name=":2" /> |
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Ranking based length, α-endorphins are the shortest with 16 amino acid residues.<ref name=":0" /> Meanwhile, the β-endorphin has the longest chain which begins with the same 16 amino acids as α-Endorphins: ]-]-Gly-]-]-]-]-]-]-Ser-]-Thr-]-]-]-Thr.<ref name=":0" /> The same sequence is also present in γ-endorphin.<ref name=":0" /> The beginning Tyr-Gly-Gly-Phe-Met chain is also known as the N-terminal pentapeptide opioid sequence.<ref name=":0" /> With such configuration, endorphins act as ]s to ]s in the brain.<ref name=":0">{{cite book | vauthors = Chaudhry SR, Gossman W | chapter = Biochemistry, Endorphin|date=2021 | chapter-url = http://www.ncbi.nlm.nih.gov/books/NBK470306/ | title = StatPearls|place=Treasure Island (FL)|publisher=StatPearls Publishing|pmid=29262177 }}</ref> |
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== Effects on behavior == |
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Studies have shown that α-endorphin is the strongest peptide in delaying ]s.<ref name=":1">{{cite book | vauthors = de Wied D | chapter = Neuropeptides in Normal and Abnormal Behavior|date=1981-01-01 | title = Endocrinology, Neuroendocrinology, Neuropeptides|pages=23–38| veditors = Stark E, Makara GB, Ács Z, Endrőczi E |publisher=Pergamon|language=en|doi=10.1016/b978-0-08-026827-9.50006-8|isbn=978-0-08-026827-9 }}</ref> α-Endorphin has the same C-terminal sequence of β-LPH, allowing these peptides to have a high affinity for opiate binding sites.<ref name=":1" /> Even a slight difference in the C-terminal amino acid can have drastic effects on avoidance behavior.<ref name=":1" /> The importance in sequencing determines the function of the endorphin.<ref name=":1" /> When an N-terminal amino acid such as tyrosine is removed, there seems to be no significant impacts on avoidance behavior.<ref name=":1" /> However, when there are adjustments to the C-terminal sequence, like removing β-LPH 61-65; activity of the endorphin decreases.<ref name=":1" /> |
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== See also == |
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* ] |
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*] |
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== References == |
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{{Reflist|2}} |
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{{Neuropeptides}} |
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{{DEFAULTSORT:Endorphin, α-}} |
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