tert-Butyl (R)-(3-(3-chlorophenyl)-1-(4-(2,5-difluorobenzoyl)piperazin-1-yl)-1-oxopropan-2-yl)carbamate | 1346949-38-9

• 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: tert-Butyl (R)-(3-(3-chlorophenyl)-1-(4-(2,5-difluorobenzoyl)piperazin-1-yl)-1-oxopropan-2-yl)carbamate
• 英文别名: tert-butyl N-[(2R)-3-(3-chlorophenyl)-1-[4-(2,5-difluorobenzoyl)piperazin-1-yl]-1-oxopropan-2-yl]carbamate
• CAS: 1346949-38-9
• 化学式: C₂₅H₂₈ClF₂N₃O₄
• 分子量: 507.965
• InChiKey: SEXNQKIFVIZLCP-OAQYLSRUSA-N

物化性质

• 沸点：
  683.1±55.0 °C(Predicted)
• 密度：
  1.303±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.04
• 重原子数：
  35.0
• 可旋转键数：
  5.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  78.95
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  tert-Butyl (R)-(3-(3-chlorophenyl)-1-(4-(2,5-difluorobenzoyl)piperazin-1-yl)-1-oxopropan-2-yl)carbamate 在 盐酸 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 以85%的产率得到(R)-2-amino-1-[4-(2,5-difluoro-benzoyl)-piperazin-1-yl]-3-(3-chloro-phenyl)-propan-1-one
  参考文献：
  名称：

  Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors

  摘要：

  Herein we report the discovery of a family of novel yet simple, amino-acid derived class I HDAC inhibitors that demonstrate isoform selectivity via access to the internal acetate release channel. Isoform selectivity criteria is discussed on the basis of X-ray crystallography and molecular modeling of these novel inhibitors bound to HDAC8, potentially revealing insights into the mechanism of enzymatic function through novel structural features revealed at the atomic level. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.06.030
• 作为产物：
  描述：

  (2,5-difluoro-phenyl)-piperazin-1-yl-methanone 、 N-叔丁氧羰基-D-3-氯苯丙氨酸 在 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 16.25h， 以92%的产率得到tert-Butyl (R)-(3-(3-chlorophenyl)-1-(4-(2,5-difluorobenzoyl)piperazin-1-yl)-1-oxopropan-2-yl)carbamate
  参考文献：
  名称：

  Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors

  摘要：

  Herein we report the discovery of a family of novel yet simple, amino-acid derived class I HDAC inhibitors that demonstrate isoform selectivity via access to the internal acetate release channel. Isoform selectivity criteria is discussed on the basis of X-ray crystallography and molecular modeling of these novel inhibitors bound to HDAC8, potentially revealing insights into the mechanism of enzymatic function through novel structural features revealed at the atomic level. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.06.030