Fmoc-D-Lys(2-Cl-Z)-OH | 1393687-43-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: Fmoc-D-Lys(2-Cl-Z)-OH
• 英文别名: (2R)-6-[(2-chlorophenyl)methoxycarbonylamino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)hexanoic acid
• CAS: 1393687-43-8
• 化学式: C₂₉H₂₉ClN₂O₆
• 分子量: 537.012
• InChiKey: VUEYAXRHPZGZOL-AREMUKBSSA-N

物化性质

• 沸点：
  769.2±60.0 °C(Predicted)
• 密度：
  1.309±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.6
• 重原子数：
  38
• 可旋转键数：
  13
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.28
• 拓扑面积：
  114
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Fmoc-D-Lys(2-Cl-Z)-OH 在 N-羟基-7-氮杂苯并三氮唑 、 1-羟基苯并三唑 、 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 苯甲醚 、 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 、 三氟乙酸 、 3-(二乙氧基邻酰氧基)-1,2,3-苯并三嗪-4-酮 、 N,N'-二异丙基碳二亚胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 3.5h， 生成
  参考文献：
  名称：

  An Hsp90 modulator that exhibits a unique mechanistic profile

  摘要：

  Described is the synthesis of two biotinylated derivatives of a cytotoxic macrocycle. Pull-down assays indicate that this macrocycle targets the N-middle domain of Hsp90. Untagged compound can effectively compete away tagged compound-Hsp90 protein complexes, confirming the binding specificity of the macrocycle for Hsp90. The macrocycle is similar in potency to other structurally-related analogs of Sansalvamide A (San A) and induces apoptosis via a caspase 3 mechanism. Unlike other San A derivatives, we show that the macrocycle does not inhibit binding between C-terminal client proteins and co-chaperones and Hsp90, suggesting that it has a unique mechanism of action. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.03.012

文献信息

• An Hsp90 modulator that exhibits a unique mechanistic profile
  作者：Deborah M. Ramsey、Jeanette R. McConnell、Leslie D. Alexander、Kaishin W. Tanaka、Chester M. Vera、Shelli R. McAlpine

  DOI：10.1016/j.bmcl.2012.03.012

  日期：2012.5

  Described is the synthesis of two biotinylated derivatives of a cytotoxic macrocycle. Pull-down assays indicate that this macrocycle targets the N-middle domain of Hsp90. Untagged compound can effectively compete away tagged compound-Hsp90 protein complexes, confirming the binding specificity of the macrocycle for Hsp90. The macrocycle is similar in potency to other structurally-related analogs of Sansalvamide A (San A) and induces apoptosis via a caspase 3 mechanism. Unlike other San A derivatives, we show that the macrocycle does not inhibit binding between C-terminal client proteins and co-chaperones and Hsp90, suggesting that it has a unique mechanism of action. (C) 2012 Elsevier Ltd. All rights reserved.