benzyl N-[(4S)-4-[[(2S)-3-methyl-2-[[(2S)-2-(methylamino)propanoyl]amino]butanoyl]amino]-5-oxo-5-[[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl]amino]pentyl]carbamate | 1446197-85-8

• 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: benzyl N-[(4S)-4-[[(2S)-3-methyl-2-[[(2S)-2-(methylamino)propanoyl]amino]butanoyl]amino]-5-oxo-5-[[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl]amino]pentyl]carbamate
• CAS: 1446197-85-8
• 化学式: C₃₂H₄₅N₅O₅
• 分子量: 579.74
• InChiKey: LAEIPUYJNBHTFF-QTMWPNOBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  42
• 可旋转键数：
  15
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  138
• 氢给体数：
  5
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  H-Orn(Z)-OBzl 在 N-甲基吗啉 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 benzyl N-[(4S)-4-[[(2S)-3-methyl-2-[[(2S)-2-(methylamino)propanoyl]amino]butanoyl]amino]-5-oxo-5-[[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl]amino]pentyl]carbamate
  参考文献：
  名称：

  Design, synthesis and evaluation of inhibitor of apoptosis protein (IAP) antagonists that are highly selective for the BIR2 domain of XIAP

  摘要：

  We recently reported the systematic ligand-based rational design and synthesis of monovalent Smac mimetics that bind preferentially to the BIR2 domain of the anti-apoptotic protein XIAP. Expanded structure-activity relationship (SAR) studies around these peptidomimetics led to compounds with significantly improved selectivity (>60-fold) for the BIR2 domain versus the BIR3 domain of XIAP. The potent and highly selective IAP antagonist 8q (ML183) sensitized TRAIL-resistant prostate cancer cells to apoptotic cell death, highlighting the merit of this probe compound as a valuable tool to investigate the biology of XIAP. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.04.096

文献信息

• Design, synthesis and evaluation of inhibitor of apoptosis protein (IAP) antagonists that are highly selective for the BIR2 domain of XIAP
  作者：Robert J. Ardecky、Kate Welsh、Darren Finlay、Pooi San Lee、Marcos González-López、Santhi Reddy Ganji、Palaniyandi Ravanan、Peter D. Mace、Stefan J. Riedl、Kristiina Vuori、John C. Reed、Nicholas D.P. Cosford

  DOI：10.1016/j.bmcl.2013.04.096

  日期：2013.7

  We recently reported the systematic ligand-based rational design and synthesis of monovalent Smac mimetics that bind preferentially to the BIR2 domain of the anti-apoptotic protein XIAP. Expanded structure-activity relationship (SAR) studies around these peptidomimetics led to compounds with significantly improved selectivity (>60-fold) for the BIR2 domain versus the BIR3 domain of XIAP. The potent and highly selective IAP antagonist 8q (ML183) sensitized TRAIL-resistant prostate cancer cells to apoptotic cell death, highlighting the merit of this probe compound as a valuable tool to investigate the biology of XIAP. (C) 2013 Elsevier Ltd. All rights reserved.