Glycylmethionine: Difference between revisions
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==Oxidation== |
==Oxidation== |
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The oxidation of Gly-Met and its reverse sequence, Met-Gly, is an interesting topic. Both photooxidation and collision-induced dissociation of Gly-Met happen through electron transfer from either the sulfur atom or the terminal amino group when it is in its uncharged state. This process leads to the formation of α-protons and sulfur-centered cation radicals in Gly-Met <ref>{{Cite web|url=https://pubmed.ncbi.nlm.nih.gov/23440718/|title=Fragmentation chemistry of [Met-Gly]•+, [Gly-Met]•+, and [Met-Met]•+ radical cations|website=https://pubs.acs.org/doi/10.1007/s13361-013-0581-5}</ref>. |
The oxidation of Gly-Met and its reverse sequence, Met-Gly, is an interesting topic. Both photooxidation and collision-induced dissociation of Gly-Met happen through electron transfer from either the sulfur atom or the terminal amino group when it is in its uncharged state. This process leads to the formation of α-protons and sulfur-centered cation radicals in Gly-Met <ref>{{Cite web|url=https://pubmed.ncbi.nlm.nih.gov/23440718/|title=Fragmentation chemistry of [Met-Gly]•+, [Gly-Met]•+, and [Met-Met]•+ radical cations|website=https://pubs.acs.org/doi/10.1007/s13361-013-0581-5}}</ref>. |
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However, the photooxidation of Met-Gly behaves differently from Gly-Met. The peptide’s conformation plays a crucial role in understanding the oxidation mechanism. In Met-Gly, the process leads to the formation of an open-chain sulfur-centered cation radical. This radical then releases a proton from the N-terminal amino group, resulting in a five-membered cyclic radical structure with a three-electron bond between the sulfur and nitrogen atoms. |
However, the photooxidation of Met-Gly behaves differently from Gly-Met. The peptide’s conformation plays a crucial role in understanding the oxidation mechanism. In Met-Gly, the process leads to the formation of an open-chain sulfur-centered cation radical. This radical then releases a proton from the N-terminal amino group, resulting in a five-membered cyclic radical structure with a three-electron bond between the sulfur and nitrogen atoms. |
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Peptides can adopt different conformations—cationic, zwitterionic, or anionic—depending on the solvent and pH. The zwitterionic form of Gly-Met is particularly important as it is responsible for the formation of sulfur-centered radicals<ref>{{Cite web|url=https://journals.iucr.org/e/issues/2024/07/00/hb8099/index.html#BB9|title=Crystal structures of the isomeric dipeptides L-glycyl-L-methionine and L-methionyl-L-glycine|website=https://journals.iucr.org/e/issues/2024/07/00/hb8099/index.html#BB9}</ref>. This same mechanism can cause similar damage in proteins. |
Peptides can adopt different conformations—cationic, zwitterionic, or anionic—depending on the solvent and pH. The zwitterionic form of Gly-Met is particularly important as it is responsible for the formation of sulfur-centered radicals<ref>{{Cite web|url=https://journals.iucr.org/e/issues/2024/07/00/hb8099/index.html#BB9|title=Crystal structures of the isomeric dipeptides L-glycyl-L-methionine and L-methionyl-L-glycine|website=https://journals.iucr.org/e/issues/2024/07/00/hb8099/index.html#BB9}}</ref>. This same mechanism can cause similar damage in proteins. |
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==References== |
==References== |
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{{reflist}} |
{{reflist}} |
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Revision as of 03:33, 17 June 2024
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| Names | |
|---|---|
| IUPAC name
L-Glycyl-L-methionine
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| Other names
(2S)-2-[(2-aminoacetyl)amino]-4-methylsulfanylbutanoic acid
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| Identifiers | |
3D model (JSmol)
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| ChEMBL | |
| ChemSpider | |
| ECHA InfoCard | 100.008.252 |
PubChem CID
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| Properties | |
| C7H14N2O3S | |
| Molar mass | 206.26 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Glycyl-methionine or Gly-Met is a dipeptide consisting of the amino acids glycine and methionine[1]. It plays a role as a metabolite. It is reverse of Methionylglycine or Met-Gly sequence.
Oxidation
The oxidation of Gly-Met and its reverse sequence, Met-Gly, is an interesting topic. Both photooxidation and collision-induced dissociation of Gly-Met happen through electron transfer from either the sulfur atom or the terminal amino group when it is in its uncharged state. This process leads to the formation of α-protons and sulfur-centered cation radicals in Gly-Met [2].
However, the photooxidation of Met-Gly behaves differently from Gly-Met. The peptide’s conformation plays a crucial role in understanding the oxidation mechanism. In Met-Gly, the process leads to the formation of an open-chain sulfur-centered cation radical. This radical then releases a proton from the N-terminal amino group, resulting in a five-membered cyclic radical structure with a three-electron bond between the sulfur and nitrogen atoms.
Peptides can adopt different conformations—cationic, zwitterionic, or anionic—depending on the solvent and pH. The zwitterionic form of Gly-Met is particularly important as it is responsible for the formation of sulfur-centered radicals[3]. This same mechanism can cause similar damage in proteins.
References
- ^ "L-Glycylmethionine". PubChem.
- ^ "Fragmentation chemistry of [Met-Gly]•+, [Gly-Met]•+, and [Met-Met]•+ radical cations". https://pubs.acs.org/doi/10.1007/s13361-013-0581-5.
{{cite web}}: External link in|website= - ^ "Crystal structures of the isomeric dipeptides L-glycyl-L-methionine and L-methionyl-L-glycine". https://journals.iucr.org/e/issues/2024/07/00/hb8099/index.html#BB9.
{{cite web}}: External link in|website=|title=at position 60 (help)