[(R)-1-(2,4-dimethylbenzyl)pyrrolidin-3-yl]carbamic acid tert-butyl ester | 603152-36-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: [(R)-1-(2,4-dimethylbenzyl)pyrrolidin-3-yl]carbamic acid tert-butyl ester
• 英文别名: tert-butyl N-[(3R)-1-[(2,4-dimethylphenyl)methyl]pyrrolidin-3-yl]carbamate
• CAS: 603152-36-9
• 化学式: C₁₈H₂₈N₂O₂
• 分子量: 304.433
• InChiKey: LJJXIQCZTODGKI-MRXNPFEDSA-N

物化性质

• 沸点：
  417.8±34.0 °C(Predicted)
• 密度：
  1.06±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  22
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  41.6
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  [(R)-1-(2,4-dimethylbenzyl)pyrrolidin-3-yl]carbamic acid tert-butyl ester 在 盐酸 、 1-羟基苯并三唑 、 N,N'-二异丙基碳二亚胺 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 19.0h， 生成 {[(R)-1-(2,4-dimethylbenzyl)pyrrolidin-3-ylcarbamoyl]methyl}carbamic acid tert-butyl ester
  参考文献：
  名称：

  CCR2:  Characterization of the Antagonist Binding Site from a Combined Receptor Modeling/Mutagenesis Approach

  摘要：

  We describe here a classical molecular modeling exercise that was carried out to provide a basis for the design of novel antagonist ligands of the CCR2 receptor. Using a theoretical model of the CCR2 receptor, docking studies were carried out to define plausible binding modes for the various known antagonist ligands, including our own series of indole piperidine compounds. On the basis of these results, a number of site-directed mutations (SDM) were designed that were intended to verify the proposed docking models. From these it was clear that further refinements would be necessary in the model. This was aided by the publication of a crystal structure of bovine enabled us to define ligand-docking hypotheses that were in complete agreement with the results of the SDM experiments.

  DOI：

  10.1021/jm030862l
• 作为产物：
  描述：

  2,4-二甲基苯甲醛 、 (R)-3-叔丁氧羰基氨基吡咯烷 在 三乙酰氧基硼氢化钠 作用下， 以 1,2-二氯乙烷 为溶剂， 反应 3.0h， 以89%的产率得到[(R)-1-(2,4-dimethylbenzyl)pyrrolidin-3-yl]carbamic acid tert-butyl ester
  参考文献：
  名称：

  CCR2:  Characterization of the Antagonist Binding Site from a Combined Receptor Modeling/Mutagenesis Approach

  摘要：

  We describe here a classical molecular modeling exercise that was carried out to provide a basis for the design of novel antagonist ligands of the CCR2 receptor. Using a theoretical model of the CCR2 receptor, docking studies were carried out to define plausible binding modes for the various known antagonist ligands, including our own series of indole piperidine compounds. On the basis of these results, a number of site-directed mutations (SDM) were designed that were intended to verify the proposed docking models. From these it was clear that further refinements would be necessary in the model. This was aided by the publication of a crystal structure of bovine enabled us to define ligand-docking hypotheses that were in complete agreement with the results of the SDM experiments.

  DOI：

  10.1021/jm030862l

文献信息

• CCR2:  Characterization of the Antagonist Binding Site from a Combined Receptor Modeling/Mutagenesis Approach
  作者：Theo A. Berkhout、Frank E. Blaney、Angela M. Bridges、David G. Cooper、Ian T. Forbes、Andrew D. Gribble、Pieter H. E. Groot、Adam Hardy、Robert J. Ife、Rejbinder Kaur、Kitty E. Moores、Helen Shillito、Jennifer Willetts、Jason Witherington

  DOI：10.1021/jm030862l

  日期：2003.9.1

  We describe here a classical molecular modeling exercise that was carried out to provide a basis for the design of novel antagonist ligands of the CCR2 receptor. Using a theoretical model of the CCR2 receptor, docking studies were carried out to define plausible binding modes for the various known antagonist ligands, including our own series of indole piperidine compounds. On the basis of these results, a number of site-directed mutations (SDM) were designed that were intended to verify the proposed docking models. From these it was clear that further refinements would be necessary in the model. This was aided by the publication of a crystal structure of bovine enabled us to define ligand-docking hypotheses that were in complete agreement with the results of the SDM experiments.