3-butyl-1-hydroxythiourea | 6919-39-7

• 分子结构分类: 有机化合物 - 有机硫化合物
• 英文名称: 3-butyl-1-hydroxythiourea
• 英文别名: N-Hydroxy-N'-butyl-thioharnstoff；1-Butyl-3-hydroxythiourea
• CAS: 6919-39-7
• 化学式: C₅H₁₂N₂OS
• mdl: MFCD08067452
• 分子量: 148.229
• InChiKey: AVKBIOXNVRXYQM-UHFFFAOYSA-N

物化性质

• 熔点：
  99-101 °C (decomp)
• 沸点：
  235.1±23.0 °C(Predicted)
• 密度：
  1.129±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  9
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  76.4
• 氢给体数：
  3
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  丁基异硫氰酸酯 在 羟胺 作用下， 以 甲醇 为溶剂， 反应 1.0h， 以95%的产率得到3-butyl-1-hydroxythiourea
  参考文献：
  名称：

  Synthesis and Evaluation of New Sulfur-Containing l-Arginine-Derived Inhibitors of Nitric Oxide Synthase

  摘要：

  A series of compounds (7, 8, 10-17, 23) containing new functional groups derived by the combination of the substrate, intermediate, product, and known inhibitors of nitric oxide synthase (NOS) were prepared and evaluated against NOS. While none of the compounds assayed acted as a nitric oxide-producing substrate, the sulfur-containing arginine derivatives 10-12 were competitive inhibitors of iNOS with K-i's of 202, 7, and 58 mu M, respectively. Compound 11 demonstrated the greatest potency against NOS-mediated citrulline formation for each of the three isoforms with IC50's of 6.7, 19.7, and 13 mu M for nNOS, eNOS, and iNOS, respectively. Compounds 10-12 each demonstrated a slight selectivity for inhibition of the neuronal isoform compared to the endothelial and inducible isoforms. These compounds also influenced the NADPH oxidase activity and heme iron spin state in a manner similar to structurally related compounds. Compound 10, a thiocarbonyl-containing compound, decreased the NADPH oxidase activity of the enzyme (EC50 = 190 mu M) and shifted the heme iron spin state toward a low-spin configuration, similar to that of L-thiocitrulline. Compounds 11 and 12, S-alkylthiocitrulline derivatives, decreased the NADPH oxidase activity of the enzyme (EC50 = 6.6 and 180 mu M, respectively) and shifted the heme iron spin state toward a high-spin configuration, similar to that of L-S-methylisothiocitrulline. Carbonyl-containing amino acid (7, 8, 23) and non-amino acid (13-17) analogues did not interact well with the enzyme.

  DOI：

  10.1021/jm980232x

文献信息

• N-substituted N'-hydroxythioureas
  作者：Gil Clifton、Sarah R. Bryant、Charles G. Skinner

  DOI：10.1021/jm00297a009

  日期：1970.5
• Zinner; Weber, Pharmazie, 1966, vol. 21, # 1, p. 23 - 25
  作者：Zinner、Weber

  DOI：——

  日期：——
• Synthesis and Evaluation of New Sulfur-Containing <scp>l</scp>-Arginine-Derived Inhibitors of Nitric Oxide Synthase
  作者：Kohji Ichimori、Dennis J. Stuehr、Robert N. Atkinson、S. Bruce King

  DOI：10.1021/jm980232x

  日期：1999.5.1

  A series of compounds (7, 8, 10-17, 23) containing new functional groups derived by the combination of the substrate, intermediate, product, and known inhibitors of nitric oxide synthase (NOS) were prepared and evaluated against NOS. While none of the compounds assayed acted as a nitric oxide-producing substrate, the sulfur-containing arginine derivatives 10-12 were competitive inhibitors of iNOS with K-i's of 202, 7, and 58 mu M, respectively. Compound 11 demonstrated the greatest potency against NOS-mediated citrulline formation for each of the three isoforms with IC50's of 6.7, 19.7, and 13 mu M for nNOS, eNOS, and iNOS, respectively. Compounds 10-12 each demonstrated a slight selectivity for inhibition of the neuronal isoform compared to the endothelial and inducible isoforms. These compounds also influenced the NADPH oxidase activity and heme iron spin state in a manner similar to structurally related compounds. Compound 10, a thiocarbonyl-containing compound, decreased the NADPH oxidase activity of the enzyme (EC50 = 190 mu M) and shifted the heme iron spin state toward a low-spin configuration, similar to that of L-thiocitrulline. Compounds 11 and 12, S-alkylthiocitrulline derivatives, decreased the NADPH oxidase activity of the enzyme (EC50 = 6.6 and 180 mu M, respectively) and shifted the heme iron spin state toward a high-spin configuration, similar to that of L-S-methylisothiocitrulline. Carbonyl-containing amino acid (7, 8, 23) and non-amino acid (13-17) analogues did not interact well with the enzyme.