benzyl N-[(12S,15S,18S)-15-benzyl-18-formyl-13,16-dioxo-2-oxa-5,6,7,14,17-pentaazatricyclo[18.2.2.1(4,7)]pentacosa-1(22),4(25),5,20,23-pentaen-12-yl]carbamate | 1359969-08-6

• 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-[(12S,15S,18S)-15-benzyl-18-formyl-13,16-dioxo-2-oxa-5,6,7,14,17-pentaazatricyclo[18.2.2.1(4,7)]pentacosa-1(22),4(25),5,20,23-pentaen-12-yl]carbamate
• 英文别名: benzyl N-[(12S,15S,18S)-15-benzyl-18-formyl-13,16-dioxo-2-oxa-5,6,7,14,17-pentazatricyclo[18.2.2.14,7]pentacosa-1(23),4(25),5,20(24),21-pentaen-12-yl]carbamate
• CAS: 1359969-08-6
• 化学式: C₃₅H₃₈N₆O₆
• 分子量: 638.723
• InChiKey: CLHWILDYKGOQGC-MHDHXZMLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  47
• 可旋转键数：
  7
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  154
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  Boc-L-酪氨酸甲酯 在 sodium tetrahydroborate 、 potassium carbonate 、 1-羟基苯并三唑 、 戴斯-马丁氧化剂 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 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 、 三氟乙酸 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 32.0h， 生成 benzyl N-[(12S,15S,18S)-15-benzyl-18-formyl-13,16-dioxo-2-oxa-5,6,7,14,17-pentaazatricyclo[18.2.2.1(4,7)]pentacosa-1(22),4(25),5,20,23-pentaen-12-yl]carbamate
  参考文献：
  名称：

  New β-Strand Templates Constrained by Huisgen Cycloaddition

  摘要：

  New peptidic templates constrained into a beta-strand geometry by linking acetylene and azide containing P-1 and P-3 residues of a tripeptide by Huisgen cycloaddition are presented. The conformations of the macrocycles are defined by NMR studies and those that best define a beta-strand are shown to be potent inhibitors of the protease calpain. The beta-strand templates presented and defined here are prepared under optimized conditions that should be suitable for targeting a range of proteases and other applications requiring such a geometry.

  DOI：

  10.1021/ol3002199

文献信息

• New β-Strand Templates Constrained by Huisgen Cycloaddition
  作者：Ashok D. Pehere、Andrew D. Abell

  DOI：10.1021/ol3002199

  日期：2012.3.2

  New peptidic templates constrained into a beta-strand geometry by linking acetylene and azide containing P-1 and P-3 residues of a tripeptide by Huisgen cycloaddition are presented. The conformations of the macrocycles are defined by NMR studies and those that best define a beta-strand are shown to be potent inhibitors of the protease calpain. The beta-strand templates presented and defined here are prepared under optimized conditions that should be suitable for targeting a range of proteases and other applications requiring such a geometry.