N-(tert-butoxycarbonyl)-5-methoxy-2-methylindoline | 899419-81-9

• 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: N-(tert-butoxycarbonyl)-5-methoxy-2-methylindoline
• 英文别名: Tert-butyl 5-methoxy-2-methyl-2,3-dihydroindole-1-carboxylate
• CAS: 899419-81-9
• 化学式: C₁₅H₂₁NO₃
• 分子量: 263.337
• InChiKey: CYAXGTMVQLUHRV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  19
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  38.8
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-(tert-butoxycarbonyl)-5-methoxy-2-methylindoline 在 三乙基硅烷 、 sodium tetrahydroborate 、 四甲基乙二胺 、 氨 、 仲丁基锂 、 三溴化硼 、 sodium hydride 、 三氟乙酸 、 2,3-二氯-5,6-二氰基-1,4-苯醌 作用下， 以 1,4-二氧六环 、 乙醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 79.5h， 生成 4-(1-Benzyl-3-carbamoylmethyl-2,7-dimethyl-1H-indol-5-yloxy)-butyric acid ethyl ester
  参考文献：
  名称：

  Indole Inhibitors of Human Nonpancreatic Secretory Phospholipase A₂. 2. Indole-3-acetamides with Additional Functionality

  摘要：

  As reported in our previous paper, a series of indole-3-acetamides which possessed potency and selectivity as inhibitors of human nonpancreatic secretory phospholipase A(2)(hnps-PLA(2)) was developed. The design of these compounds was based on information derived from x-ray crystal structures determined for complexes between the enzyme and its inhibitors. We describe here the further implementation of this structure-based design strategy and continued SAR development to produce indole-3-acetamides with additional functionalities which provide increased interaction with important residues within the enzyme active site. These efforts led to inhibitors with substantially enhanced potency and selectivity.

  DOI：

  10.1021/jm960486n
• 作为产物：
  描述：

  5-甲氧基-2-甲基吲哚 在 sodium hydroxide 、 sodium cyanoborohydride 、 溶剂黄146 作用下， 以 四氢呋喃 为溶剂， 反应 26.0h， 生成 N-(tert-butoxycarbonyl)-5-methoxy-2-methylindoline
  参考文献：
  名称：

  Indole Inhibitors of Human Nonpancreatic Secretory Phospholipase A₂. 2. Indole-3-acetamides with Additional Functionality

  摘要：

  As reported in our previous paper, a series of indole-3-acetamides which possessed potency and selectivity as inhibitors of human nonpancreatic secretory phospholipase A(2)(hnps-PLA(2)) was developed. The design of these compounds was based on information derived from x-ray crystal structures determined for complexes between the enzyme and its inhibitors. We describe here the further implementation of this structure-based design strategy and continued SAR development to produce indole-3-acetamides with additional functionalities which provide increased interaction with important residues within the enzyme active site. These efforts led to inhibitors with substantially enhanced potency and selectivity.

  DOI：

  10.1021/jm960486n

文献信息

• Ru-NHC-Catalyzed Asymmetric, Complete Hydrogenation of Indoles and Benzofurans: One Catalyst with Dual Function
  作者：Fuhao Zhang、Himadri Sekhar Sasmal、Constantin G. Daniliuc、Frank Glorius

  DOI：10.1021/jacs.3c04983

  日期：2023.7.26

  The highly enantioselective and complete hydrogenation of protected indoles and benzofurans has been developed, affording facile access to a range of chiral three-dimensional octahydroindoles and octahydrobenzofurans, which are prevalent in many bioactive molecules and organocatalysts. Remarkably, we are in control of the nature of the ruthenium N-heterocyclic carbene complex and employed the complex

  受保护的吲哚和苯并呋喃的高度对映选择性和完全氢化已经被开发出来，可以方便地获得一系列手性三维八氢吲哚和八氢苯并呋喃，它们在许多生物活性分子和有机催化剂中普遍存在。值得注意的是，我们控制了钌N-杂环卡宾配合物的性质，并将该配合物用作均相和非均相催化剂，为其在更具挑战性的芳香族化合物的不对称氢化中的潜在应用提供了新途径。
• Indole Inhibitors of Human Nonpancreatic Secretory Phospholipase A₂. 2. Indole-3-acetamides with Additional Functionality
  作者：Robert D. Dillard、Nicholas J. Bach、Susan E. Draheim、Dennis R. Berry、Donald G. Carlson、Nickolay Y. Chirgadze、David K. Clawson、Lawrence W. Hartley、Lea M. Johnson、Noel D. Jones、Emma R. McKinney、Edward D. Mihelich、Jennifer L. Olkowski、Richard W. Schevitz、Amy C. Smith、David W. Snyder、Cynthia D. Sommers、Jean-Pierre Wery

  DOI：10.1021/jm960486n

  日期：1996.1.1

  As reported in our previous paper, a series of indole-3-acetamides which possessed potency and selectivity as inhibitors of human nonpancreatic secretory phospholipase A(2)(hnps-PLA(2)) was developed. The design of these compounds was based on information derived from x-ray crystal structures determined for complexes between the enzyme and its inhibitors. We describe here the further implementation of this structure-based design strategy and continued SAR development to produce indole-3-acetamides with additional functionalities which provide increased interaction with important residues within the enzyme active site. These efforts led to inhibitors with substantially enhanced potency and selectivity.