(S)-6-Benzyloxycarbonylamino-2-(4-hydroxy-benzoylamino)-hexanoic acid methyl ester | 216880-29-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (S)-6-Benzyloxycarbonylamino-2-(4-hydroxy-benzoylamino)-hexanoic acid methyl ester
• CAS: 216880-29-4
• 化学式: C₂₂H₂₆N₂O₆
• 分子量: 414.458
• InChiKey: XSOWUYNWINRJOX-IBGZPJMESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.76
• 重原子数：
  30.0
• 可旋转键数：
  10.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  113.96
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (S)-6-Benzyloxycarbonylamino-2-(4-hydroxy-benzoylamino)-hexanoic acid methyl ester 在 sodium hydroxide 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 反应 6.5h， 生成 [(S)-5-(4-Hydroxy-benzoylamino)-5-(4-hydroxy-phenylcarbamoyl)-pentyl]-carbamic acid benzyl ester
  参考文献：
  名称：

  Enzyme-Controlled Molecular Recognition:  Selective Targeting of Trypsin with a Substrate-Inhibitor Supramolecular Complex

  摘要：

  We have synthesized and studied the host compound (1) that forms a noncovalent complex (K = 480 +/- 30 M-1) with 1,4-diamidinobenzene (2) at pD 8.0 in D2O. Guest 2 has been shown to inhibit the proteases specific for cationic side chains (Ki values for thrombin,plasmin, and trypsin being 1.0 +/- 0.4, 0.6 +/- 0.1, and 0.88 +/- 0.07 mM, respectively). Host 1 and the 1.2 complex are shown to undergo the trypsin-catalyzed cleavage that results in the increased concentration of the free form of 2 and, therefore, induces the enzyme inhibition. Plasmin and thrombin are shown to cleave I at a significantly lower rate than trypsin. Thus, the complex of 1 with 2 represents the first example of a selective enzyme-sensitive supramolecular system capable of enzyme targeting through a "trojan horse"-type mechanism in which a bioactive compound acts on the same molecule that provides its release from a delivery system.

  DOI：

  10.1021/ja980810z
• 作为产物：
  描述：

  (S)-methyl 2-amino-6-(benzyloxycarbonylamino)hexanoate 、 对羟基苯甲酸 在 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 为溶剂， 反应 4.0h， 以69%的产率得到(S)-6-Benzyloxycarbonylamino-2-(4-hydroxy-benzoylamino)-hexanoic acid methyl ester
  参考文献：
  名称：

  Enzyme-Controlled Molecular Recognition:  Selective Targeting of Trypsin with a Substrate-Inhibitor Supramolecular Complex

  摘要：

  We have synthesized and studied the host compound (1) that forms a noncovalent complex (K = 480 +/- 30 M-1) with 1,4-diamidinobenzene (2) at pD 8.0 in D2O. Guest 2 has been shown to inhibit the proteases specific for cationic side chains (Ki values for thrombin,plasmin, and trypsin being 1.0 +/- 0.4, 0.6 +/- 0.1, and 0.88 +/- 0.07 mM, respectively). Host 1 and the 1.2 complex are shown to undergo the trypsin-catalyzed cleavage that results in the increased concentration of the free form of 2 and, therefore, induces the enzyme inhibition. Plasmin and thrombin are shown to cleave I at a significantly lower rate than trypsin. Thus, the complex of 1 with 2 represents the first example of a selective enzyme-sensitive supramolecular system capable of enzyme targeting through a "trojan horse"-type mechanism in which a bioactive compound acts on the same molecule that provides its release from a delivery system.

  DOI：

  10.1021/ja980810z