2-(cyclopentylmethyl-((2S)-2-((2-methoxyphenyl)carbamoylamino)-3,3-dimethyl-butanoyl)amino)acetic acid ethyl ester | 1242177-67-8

• 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: 2-(cyclopentylmethyl-((2S)-2-((2-methoxyphenyl)carbamoylamino)-3,3-dimethyl-butanoyl)amino)acetic acid ethyl ester
• CAS: 1242177-67-8
• 化学式: C₂₄H₃₇N₃O₅
• 分子量: 447.575
• InChiKey: NGKRXXOENMXBNW-OAQYLSRUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.81
• 重原子数：
  32.0
• 可旋转键数：
  9.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  96.97
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  2-(cyclopentylmethyl-((2S)-2-((2-methoxyphenyl)carbamoylamino)-3,3-dimethyl-butanoyl)amino)acetic acid ethyl ester 在 羟胺 作用下， 以 甲醇 为溶剂， 反应 2.0h， 以0.022 g的产率得到(2S)-N-(cyclopentylmethyl)-N-(2-(hydroxyamino)-2-oxo-ethyl)-2-((2-methoxyphenyl)carbamoylamino)-3,3-dimethyl-butanamide
  参考文献：
  名称：

  Peptide deformylase inhibitors with retro-amide scaffold: Synthesis and structure–activity relationships

  摘要：

  Peptide deformylase (PDF) is a metalloprotease catalyzing the removal of a formyl group from newly synthesized proteins. Thus inhibition of PDF activity is considered to be one of the most effective antibiotic strategies. Reported herein are the synthesis and structure-activity relationship studies of retro-amide inhibitors based on actinonin, a naturally occurring PDF inhibitor. Analysis of the structure-activity relationships led to the discovery of 7a, which exhibits potent enzyme inhibition and antibacterial activity against Streptococcus pneumoniae, Haemophilus influenzae, and Moraxella catarrhalis. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.06.088
• 作为产物：
  描述：

  ((1S)-1-(cyclopentylmethyl-(2-ethoxy-oxo-ethyl)carbamoyl)-2,2-dimethyl-propyl)ammonium chloride 、 2-甲氧基苯基异氰酸酯 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 18.0h， 以64.3%的产率得到2-(cyclopentylmethyl-((2S)-2-((2-methoxyphenyl)carbamoylamino)-3,3-dimethyl-butanoyl)amino)acetic acid ethyl ester
  参考文献：
  名称：

  Peptide deformylase inhibitors with retro-amide scaffold: Synthesis and structure–activity relationships

  摘要：

  Peptide deformylase (PDF) is a metalloprotease catalyzing the removal of a formyl group from newly synthesized proteins. Thus inhibition of PDF activity is considered to be one of the most effective antibiotic strategies. Reported herein are the synthesis and structure-activity relationship studies of retro-amide inhibitors based on actinonin, a naturally occurring PDF inhibitor. Analysis of the structure-activity relationships led to the discovery of 7a, which exhibits potent enzyme inhibition and antibacterial activity against Streptococcus pneumoniae, Haemophilus influenzae, and Moraxella catarrhalis. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2010.06.088