4-[[5-(5-Chlorothiophen-2-yl)-1,2-oxazol-3-yl]methyl]-1-[10-[4-[[5-(5-chlorothiophen-2-yl)-1,2-oxazol-3-yl]methyl]-2-oxopiperazin-1-yl]decyl]piperazin-2-one | 1374037-21-4

• 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-[[5-(5-Chlorothiophen-2-yl)-1,2-oxazol-3-yl]methyl]-1-[10-[4-[[5-(5-chlorothiophen-2-yl)-1,2-oxazol-3-yl]methyl]-2-oxopiperazin-1-yl]decyl]piperazin-2-one
• CAS: 1374037-21-4
• 化学式: C₃₄H₄₂Cl₂N₆O₄S₂
• 分子量: 733.783
• InChiKey: WYTHFLDDCOTYIK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.1
• 重原子数：
  48
• 可旋转键数：
  17
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  156
• 氢给体数：
  0
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  2-乙酰基-5-氯噻酚 在 sodium tetrahydroborate 、 盐酸羟胺 、 sodium hydride 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 1-(10-chlorodecyl)-4-((5-(5-chlorothiophen-2-yl)isoxazol-3-yl)methyl)piperazin-2-one 、 4-[[5-(5-Chlorothiophen-2-yl)-1,2-oxazol-3-yl]methyl]-1-[10-[4-[[5-(5-chlorothiophen-2-yl)-1,2-oxazol-3-yl]methyl]-2-oxopiperazin-1-yl]decyl]piperazin-2-one
  参考文献：
  名称：

  Dimerization of β-tryptase inhibitors, does it work for both basic and neutral P1 groups?

  摘要：

  The tetrameric folding of beta-tryptase and the pair-wise distribution of its substrate binding sites offer a unique opportunity for development of inhibitors that span two adjacent binding sites. A series of dimeric inhibitors with two basic P1 moieties was discovered using this design strategy and exhibited tight-binder characteristics. Using the same strategy, an attempt was made to design and synthesize dimeric inhibitors with two neutral-P1 groups in hope to exploit the dimeric binding mode to achieve a starting point for further optimization. The unsuccessful attempt, however, demonstrated the important role played by Ala190 in neutral-P1 binding and casted further doubt on the possibility of developing neutral-P1 inhibitors for beta-tryptase. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.01.021

文献信息

• Dimerization of β-tryptase inhibitors, does it work for both basic and neutral P1 groups?
  作者：Guyan Liang、Yong Mi Choi-Sledeski、Xin Chen、Yong Gong、Eric W. MacMillan、Joseph Tsay、Keith Sides、Jennifer Cairns、Berndt Kulitzscher、David J. Aldous、Isabelle Morize、Henry W. Pauls

  DOI：10.1016/j.bmcl.2012.01.021

  日期：2012.5

  The tetrameric folding of beta-tryptase and the pair-wise distribution of its substrate binding sites offer a unique opportunity for development of inhibitors that span two adjacent binding sites. A series of dimeric inhibitors with two basic P1 moieties was discovered using this design strategy and exhibited tight-binder characteristics. Using the same strategy, an attempt was made to design and synthesize dimeric inhibitors with two neutral-P1 groups in hope to exploit the dimeric binding mode to achieve a starting point for further optimization. The unsuccessful attempt, however, demonstrated the important role played by Ala190 in neutral-P1 binding and casted further doubt on the possibility of developing neutral-P1 inhibitors for beta-tryptase. (C) 2012 Elsevier Ltd. All rights reserved.