tert-butyl N-[(2S)-1-[2-[4-(3,4-dihydro-2H-quinolin-1-yl)-4-oxobutanoyl]hydrazinyl]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]carbamate | 1043899-50-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: tert-butyl N-[(2S)-1-[2-[4-(3,4-dihydro-2H-quinolin-1-yl)-4-oxobutanoyl]hydrazinyl]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]carbamate
• CAS: 1043899-50-8
• 化学式: C₂₉H₃₅N₅O₅
• 分子量: 533.627
• InChiKey: BYRKNLXXFYKEET-QHCPKHFHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  39
• 可旋转键数：
  9
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  133
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  Boc(L)-色氨酰肼 、 4-(3,4-二氢-1(2H)-喹啉基)-4-氧代丁酸 在 4-二甲氨基吡啶 、 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 tert-butyl N-[(2S)-1-[2-[4-(3,4-dihydro-2H-quinolin-1-yl)-4-oxobutanoyl]hydrazinyl]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]carbamate
  参考文献：
  名称：

  Design, synthesis, and evaluation of inhibitors of cathepsin L: Exploiting a unique thiocarbazate chemotype

  摘要：

  Recently, we identified a thiocarbazate that exhibits potent inhibitory activity against human cathepsin L. Since this structure represents a novel chemotype with potential for activity against the entire cysteine protease family, we designed, synthesized, and assayed a series of analogs to probe the mechanism of action, as well as the structural requirements for cathepsin L activity. Molecular docking studies using coordinates of a papain-inhibitor complex as a model for cathepsin L provided useful insights. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2008.04.065

文献信息

• Design, synthesis, and evaluation of inhibitors of cathepsin L: Exploiting a unique thiocarbazate chemotype
  作者：Michael C. Myers、Parag P. Shah、Mary Pat Beavers、Andrew D. Napper、Scott L. Diamond、Amos B. Smith、Donna M. Huryn

  DOI：10.1016/j.bmcl.2008.04.065

  日期：2008.6

  Recently, we identified a thiocarbazate that exhibits potent inhibitory activity against human cathepsin L. Since this structure represents a novel chemotype with potential for activity against the entire cysteine protease family, we designed, synthesized, and assayed a series of analogs to probe the mechanism of action, as well as the structural requirements for cathepsin L activity. Molecular docking studies using coordinates of a papain-inhibitor complex as a model for cathepsin L provided useful insights. (C) 2008 Elsevier Ltd. All rights reserved.