4-(3-Acetylsulfanyl-2-tert-butoxycarbonylamino-propyl)-cyclohexanecarboxylic acid ethyl ester | 156144-04-6

• 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: 4-(3-Acetylsulfanyl-2-tert-butoxycarbonylamino-propyl)-cyclohexanecarboxylic acid ethyl ester
• 英文别名: Ethyl 4-[3-acetylsulfanyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]propyl]cyclohexane-1-carboxylate
• CAS: 156144-04-6
• 化学式: C₁₉H₃₃NO₅S
• 分子量: 387.541
• InChiKey: XGHMKFGFTUFCKU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  26
• 可旋转键数：
  11
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.84
• 拓扑面积：
  107
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  4-(3-Acetylsulfanyl-2-tert-butoxycarbonylamino-propyl)-cyclohexanecarboxylic acid ethyl ester 在 sodium hydroxide 、 碘 、 苯甲醚 作用下， 以 二氯甲烷 为溶剂， 反应 6.0h， 生成 (R,S)-1,1'-dithiobis<2-amino-3-(4-carboxycyclohexyl)propane>, bis(trifluoroacetate)
  参考文献：
  名称：

  Investigation of the Active Site of Aminopeptidase A Using a Series of New Thiol-Containing Inhibitors

  摘要：

  Aminopeptidase A (APA) and aminopeptidase N (APN) are two metallopeptidases which have been suggested to be involved in the enzymatic cascade of the renin-angiotensin system. APA liberates angotensin III from angiotensin II by releasing the N-terminal aspartate, and APN participates in the inactivation of angiotensin III. As the role of angiotensin III in the regulation of blood pressure in the central nervous system and at the periphery is controversial, it was of interest to develop selective and efficient inhibitors of APA. Starting from Glu-thiol,(1) which was the first efficient APA inhibitor described, but however is equipotent on APA (K-i = 0.14 mu M) and APN (K-i = 0.12 mu M), beta-amino thiols bearing various carboxyalkyl chains have been synthesized and their inhibitory potencies measured on both purified enzymes. Compounds containing a carboxylated aromatic ring inhibited APA and APN with K-i values in the micromolar range but were slightly more active on APA. Conversely, inhibitors containing a cyclohexyl ring were more efficient on APN. Various modifications of the structure of Glu-thiol decreased inhibitory activity on both enzymes but increased the selectivity for APA, and compound 9d ((S)-4-amino-6-mercaptohexanoic acid) was 23 times more potent on APA (K-i = 2.0 mu M) than on APN (K-i = 45 mu M).

  DOI：

  10.1021/jm00035a014
• 作为产物：
  描述：

  4-羧基苯丙氨酸盐酸盐 在 platinum(IV) oxide sodium tetrahydroborate 、 氯化亚砜 、 偶氮二甲酸二异丙酯 、 氢气 、 溶剂黄146 、 三苯基膦 作用下， 以 四氢呋喃 、 乙醇 、 水 、 N,N-二甲基甲酰胺 为溶剂， 25.0~80.0 ℃ 、8.0 MPa 条件下， 反应 4.0h， 生成 4-(3-Acetylsulfanyl-2-tert-butoxycarbonylamino-propyl)-cyclohexanecarboxylic acid ethyl ester
  参考文献：
  名称：

  Investigation of the Active Site of Aminopeptidase A Using a Series of New Thiol-Containing Inhibitors

  摘要：

  Aminopeptidase A (APA) and aminopeptidase N (APN) are two metallopeptidases which have been suggested to be involved in the enzymatic cascade of the renin-angiotensin system. APA liberates angotensin III from angiotensin II by releasing the N-terminal aspartate, and APN participates in the inactivation of angiotensin III. As the role of angiotensin III in the regulation of blood pressure in the central nervous system and at the periphery is controversial, it was of interest to develop selective and efficient inhibitors of APA. Starting from Glu-thiol,(1) which was the first efficient APA inhibitor described, but however is equipotent on APA (K-i = 0.14 mu M) and APN (K-i = 0.12 mu M), beta-amino thiols bearing various carboxyalkyl chains have been synthesized and their inhibitory potencies measured on both purified enzymes. Compounds containing a carboxylated aromatic ring inhibited APA and APN with K-i values in the micromolar range but were slightly more active on APA. Conversely, inhibitors containing a cyclohexyl ring were more efficient on APN. Various modifications of the structure of Glu-thiol decreased inhibitory activity on both enzymes but increased the selectivity for APA, and compound 9d ((S)-4-amino-6-mercaptohexanoic acid) was 23 times more potent on APA (K-i = 2.0 mu M) than on APN (K-i = 45 mu M).

  DOI：

  10.1021/jm00035a014