S-Methylglutathione
(Synonyms: S-甲基谷胱甘肽) 目录号 : GC60342
S-Methylglutathione 是一种 S 取代的谷胱甘肽，一种比 GSH 更强的亲核试剂 (nucleophile)。S-Methylglutathione 对乙二醛酶 1 (glyoxalase 1) 有抑制作用。
Cas No.:2922-56-7
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
S-Methylglutathione is an S-substitued glutathione and a stronger nucleophile than GSH[1]. S-Methylglutathione has inhibitory effect on glyoxalase 1[2].
S-Methylglutathione (GS-Me) is a stronger nucleophile than GSH, which is rationalized by the more positive inductive effect of the methyl group[1].
[1]. Foye WO, et al. Synthesis and evaluation of N-alkanoyl-S-benzyl-L-cysteinylglutamic acid esters as glyoxalase I inhibitors and anticancer agents. J Pharm Sci. 1984 Apr;73(4):559-61. [2]. Milos I. Djuran,et al. Reactivity of chloro- and aqua(diethylenetriamine)platinum(II) ions with glutathione, S-methylglutathione, and guanosine 5'-monophosphate in relation to the antitumor activity and toxicity of platinum complexes. Inorg. Chem. 1991, 30, 12, 2648-2652
| Cas No. | 2922-56-7 | SDF | |
| 别名 | S-甲基谷胱甘肽 | ||
| Canonical SMILES | O=C(O)CNC([C@H](CSC)NC(CC[C@@H](C(O)=O)N)=O)=O | ||
| 分子式 | C11H19N3O6S | 分子量 | 321.35 |
| 溶解度 | Water: 35.71 mg/mL (111.12 mM) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 3.1119 mL | 15.5594 mL | 31.1187 mL |
| 5 mM | 0.6224 mL | 3.1119 mL | 6.2237 mL |
| 10 mM | 0.3112 mL | 1.5559 mL | 3.1119 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Sulfur radical cation-peptide bond complex in the one-electron oxidation of S-Methylglutathione
J Am Chem Soc 2007 Jul 25;129(29):9236-45.PMID:17602483DOI:10.1021/ja072301f.
Neighboring group participation was investigated in the *OH-induced oxidation of S-Methylglutathione in aqueous solutions. Nanosecond pulse radiolysis was used to obtain the spectra of the reaction intermediates and their kinetics. Depending on the pH, and the concentration of S-Methylglutathione, pulse irradiation leads to different transients. The transients observed were an intramolecularly bonded [>S thereforeNH2]+ intermediate, intermolecularly S thereforeS-bonded radical cation, alpha-(alkylthio)alkyl radicals, alpha-amino-alkyl-type radical, and an intramolecularly (S thereforeO)+-bonded intermediate. The latter radical is of particular note in that it supports recent observations of sulfur radical cations complexed with the oxygen atoms of peptide bonds and thus has biological and medical implications. This (S thereforeO)+-bonded intermediate had an absorption maximum at 390 nm, and we estimated its formation rate to be >or=6x10(7) s(-1). It is in equilibrium with the intermolecularly S thereforeS-bonded radical cation, and they decay together on the time scale of a few hundred microseconds. The S thereforeS-bonded radical cation is formed from the monomeric sulfur radical cation (>S*+) and an unoxidized S-Methylglutathione molecule with the rate constant of 1.0x10(9) M(-1) s(-1). The short-lived [>S thereforeNH2]+ intermediate is a precursor of decarboxylation, absorbs at approximately 390 nm, and decays on the time scale of hundreds of nanoseconds. Additional insight into the details of the association of sulfur radical cations with the oxygen atoms of the peptide bonds was gained by comparing the behavior of the S-Methylglutathione (S thereforeO+-bonded five-membered ring) with the peptide gamma-Glu-Met-Gly (S thereforeO+-bonded six-membered ring). Conclusions from experimental observations were supported by molecular modeling calculations.
Specific S-Methylglutathione incorporation into a nematocyst-rich fraction of hydra
Biochim Biophys Acta 1980 May 7;629(2):338-48.PMID:6248121DOI:10.1016/0304-4165(80)90106-3.
1. Specific S-[C]methylglutathione incorporation from Hydra japonica into a nematocyst-rich subcellular fraction was observed. 2. This specific incorporation is not rapid reversible binding, as shown by the lack of saturation of the reaction with time. 3. Saturating kinetics of specific incorporation rate with S-[14C]methylglutathione concentration suggests the existence of intermediate reversible complex between a macromolecular and S-[14C]methylglutathione. 4. Activity of specific incorporation could be solubilized by Triton X-100 treatment of the nematocyst fraction, showing that the incorporation is not due to transport processes. 5. The incorporation was markedly diminished by the addition of cold trichloroacetic acid or urea, or by heat-treatment after the incorporation, showing that the complex is not stabilized by chemical bonding. 6. No chemical changes of free S-[14C]methylglutathione were detected in the reaction mixture, showing that the macromolecule interacting with S-[14C]methylglutathione is not a catalyzing enzyme. 7. These results suggest that this is a new type of glutathione incorporation and could be explained by a type of receptor protein which accumulates glutathione molecules.
Sensitized photooxidation of S-Methylglutathione in aqueous solution: intramolecular (S∴O) and (S∴N) bonded species
J Phys Chem B 2013 Feb 28;117(8):2359-68.PMID:23347005DOI:10.1021/jp312184e.
Nanosecond laser flash photolysis was used to generate sulfur radical cations of the thioether, S-Methylglutathione (S-Me-Glu), via the one-electron oxidation of this thioether by triplet 4-carboxybenzophenone. The purpose of this investigation was to follow the neighboring group effects resulting from the interactions between the sulfur radical cationic sites and nearby lone-pair electrons on heteroatoms within the radical cation, especially the electron lone-pairs on heteroatoms in the peptide bonds. The tripeptide, S-Me-Glu, offers several possible competing neighboring group effects that are characterized in this work. Quantum yields of the various radicals and three-electron bonded (both intramolecular and intermolecular) species were determined. The pH dependence of photoinduced decarboxylation yields was used as evidence for the identification of a nine-membered ring, sulfur-nitrogen, three-electron bonded species. The mechanisms of the secondary reactions of the radicals and radical cations were characterized by resolving their overlapping transient-absorption spectra and following their kinetic behavior. In particular, sulfur-oxygen and sulfur-nitrogen three-electron bonded species were identified where the oxygen and nitrogen atoms were in the peptide bonds.
Suppression of S-methylglutathione-induced tentacle ball formation by peptides and nullification of the suppression by TGF-beta in Hydra
Chem Senses 2000 Apr;25(2):173-80.PMID:10781024DOI:10.1093/chemse/25.2.173.
Tentacle ball formation (TBF) in Hydra elicited by S-Methylglutathione (GSM) was modulated by a number of biologically active peptides. Hydra fed on Artemia, which had been hatched in a common salt solution supplemented with LiCl and ZnCl(2), easily induced TBF in response to GSM after pretreatment with trypsin. After Hydra were treated with 100 pg/ml trypsin for 10 min, the response to GSM (TBF) was sensitively suppressed by acidic fibroblast growth factor and other biologically active peptides for >10 h. Various peptides, but not transforming growth factor beta (TGF-beta), suppressed GSM-induced TBF in a specific pattern for each peptide. However, TGF-beta was unique in that it did not suppress the response to GSM, but nullified the suppressive effect of other peptides. Only active TGF-beta nullified the suppressive effect of the peptides, and the latent form of TGF-beta neither suppressed GSM-induced TBF nor nullified the suppressive effect of other peptides. Members of the TGF-beta family suppressed GSM-induced TBF. These results indicate that all peptides examined, except for TGF-beta suppressed the response to GSM in a manner specific to each peptide. This assay system would be useful in identification of biologically active peptides.
High-performance liquid chromatography/fluorescence detection of S-Methylglutathione formed by glutathione-S-transferase T1 in vitro
Arch Toxicol 2001 Feb;74(12):760-7.PMID:11305778DOI:10.1007/s002040000201.
Glutathione-S-transferase T1 (GSTT1-1) is a major isoenzyme for the biotransformation of halomethanes. The enzyme activity is located, among other places, in human liver and erythrocytes and is subject to a genetic polymorphism. Metabolism of the halomethanes via GSTT1-1 yields S-Methylglutathione (MeSG). A new HPLC assay for the enzymatic formation of MeSG was developed. The glutathione conjugate was derivatized with 9-fluorenylmethyl chloroformate, followed by reverse-phase HPLC with gradient elution and fluorescence detection. The limit of detection was as low as about 39 pmol MeSG on-column. Including derivatization and HPLC analysis, samples could be run at 42-min intervals, thus enabling a high sample throughput. The entire method was validated for analyte recovery (78.2%) and for variations in detector response with replicated injections (11.8%) and with analyses on each of 11 consecutive days (15.2%) with erythrocyte lysate incubations as the matrix. The time-, protein-, and substrate-dependences of the enzymatic catalysis with the model substrates methyl bromide (MeBr) and methyl chloride (MeCl) were studied. Due to its strong electrophilic character, MeBr caused a high level of spontaneous MeSG formation from glutathione in a protein-free medium and a substrate-trapping side reaction in the presence of proteins. Therefore, enzymatic MeSG formation rates may only be determined with MeBr concentrations of at least 3000 ppm in the presence of limited amounts of protein (e.g. 100 microl erythrocyte lysate). In contrast, MeCl showed a lower alkylating potential allowing enzymatic catalysis to be the dominant reaction in incubations with 10,000 ppm MeCl and 2 ml erythrocyte lysate.