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Names | |
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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)
|
|
Abbreviations | gly-met |
ChEBI |
|
ChEMBL | |
ChemSpider | |
ECHA InfoCard | 100.008.252 |
EC Number |
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PubChem
CID
|
|
UNII | |
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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).
|
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.
The oxidation of Gly-Met and its reverse sequence, Met-Gly, has differences. 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.
![]() | |
Names | |
---|---|
IUPAC name
L-Glycyl-L-methionine
| |
Other names
(2S)-2-[(2-aminoacetyl)amino]-4-methylsulfanylbutanoic acid
| |
Identifiers | |
3D model (
JSmol)
|
|
Abbreviations | gly-met |
ChEBI |
|
ChEMBL | |
ChemSpider | |
ECHA InfoCard | 100.008.252 |
EC Number |
|
PubChem
CID
|
|
UNII | |
| |
| |
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).
|
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.
The oxidation of Gly-Met and its reverse sequence, Met-Gly, has differences. 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.