S-Ethylthio-L-cystein | 15579-03-0

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: S-Ethylthio-L-cystein
• 英文别名: (2S)-2-amino-3-(ethyldisulfanyl)propanoic acid
• CAS: 15579-03-0；17885-24-4
• 化学式: C₅H₁₁NO₂S₂
• 分子量: 181.28
• InChiKey: YIMFYOCZTDBZJL-SCSAIBSYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.3
• 重原子数：
  10
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  114
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  5,5-dimethyl-2-thiono-1,3,2-dioxaphosphorinanyl-2-disulfanylethane 、 D-cysteine 在 三乙胺 作用下， 以 乙醇 、 水 为溶剂， 生成 S-Ethylthio-L-cystein
  参考文献：
  名称：

  S-Alk(en)ylmercaptocysteine: Chemical Synthesis, Biological Activities, and Redox-Related Mechanism

  摘要：

  S-Alk(en)ylmercaptocysteine (CySSR, R = methyl, ethyl, propyl, 1-propenyl, and ally!), which are the putative metabolites of Allium thiosulfinates, were chemically synthesized. CySSR, but not the corresponding monosulfide species S-alk(en)yl cysteine (CySR), were able to induce quinone reductase (QR, a representative phase II enzyme) in Hepa 1c1c7 cells and inhibit nitric oxide (NO, an inflammatory biomarker) formation in lipopolysaccharide (LPS)-activated RAW 264.7 cells. These results indicate the importance of the disulfide bond for the biological activities of CySSR. Glutathione (GSH) and N-acetylcysteine (NAC), but not other types of cellular antioxidants, suppressed multiple biological activities of CySSR in vitro. The inhibitory effects of GSH and NAC on the biological activities of CySSR were correlated with a glutaredoxin (Grx)-dependent intracellular reduction of CySSR to generate cysteine and RSH, which were secreted into the extracellular medium.

  DOI：

  10.1021/jf305486q

文献信息

• <i>S</i>-Alk(en)ylmercaptocysteine: Chemical Synthesis, Biological Activities, and Redox-Related Mechanism
  作者：Guodong Zhang、Kirk L. Parkin

  DOI：10.1021/jf305486q

  日期：2013.2.27

  S-Alk(en)ylmercaptocysteine (CySSR, R = methyl, ethyl, propyl, 1-propenyl, and ally!), which are the putative metabolites of Allium thiosulfinates, were chemically synthesized. CySSR, but not the corresponding monosulfide species S-alk(en)yl cysteine (CySR), were able to induce quinone reductase (QR, a representative phase II enzyme) in Hepa 1c1c7 cells and inhibit nitric oxide (NO, an inflammatory biomarker) formation in lipopolysaccharide (LPS)-activated RAW 264.7 cells. These results indicate the importance of the disulfide bond for the biological activities of CySSR. Glutathione (GSH) and N-acetylcysteine (NAC), but not other types of cellular antioxidants, suppressed multiple biological activities of CySSR in vitro. The inhibitory effects of GSH and NAC on the biological activities of CySSR were correlated with a glutaredoxin (Grx)-dependent intracellular reduction of CySSR to generate cysteine and RSH, which were secreted into the extracellular medium.