(R)-2-(Benzyloxyamino-methyl)-hex-4-ynoic acid ((S)-1-dimethylcarbamoyl-2,2-dimethyl-propyl)-amide | 607715-16-2

• 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: (R)-2-(Benzyloxyamino-methyl)-hex-4-ynoic acid ((S)-1-dimethylcarbamoyl-2,2-dimethyl-propyl)-amide
• CAS: 607715-16-2
• 化学式: C₂₂H₃₃N₃O₃
• 分子量: 387.522
• InChiKey: WPKVPGCUWUKMJY-RTBURBONSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.36
• 重原子数：
  28.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  70.67
• 氢给体数：
  2.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  (R)-2-(Benzyloxyamino-methyl)-hex-4-ynoic acid ((S)-1-dimethylcarbamoyl-2,2-dimethyl-propyl)-amide 在 palladium on activated charcoal 氢气 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 生成 (R)-2-[(Formyl-hydroxy-amino)-methyl]-hex-4-ynoic acid ((S)-1-dimethylcarbamoyl-2,2-dimethyl-propyl)-amide
  参考文献：
  名称：

  Structure–activity relationships of the peptide deformylase inhibitor BB-3497: modification of the methylene spacer and the P1′ side chain

  摘要：

  Structural modifications to the peptide deformylase inhibitor BB-3497 are described. In this paper, we describe the initial SAR around this lead for modifications to the methylene spacer and the P1' side chain. Enzyme inhibition and antibacterial activity data revealed that the optimum distance between the N-formyl hydroxylamine metal binding group and the P1' side chain is one unsubstituted methylene unit. Additionally, lipophilic P1' side chains that closely mimic the methionine residue in the substrate provided compounds with the best microbiological profile. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(03)00532-8
• 作为产物：
  描述：

  2-Formyl-hex-4-ynoic acid ethyl ester 在 sodium hydroxide 、 N-羟基-7-氮杂苯并三氮唑 、 sodium acetate 、 sodium cyanoborohydride 、 溶剂黄146 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 作用下， 以 甲醇 、 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 生成 (R)-2-(Benzyloxyamino-methyl)-hex-4-ynoic acid ((S)-1-dimethylcarbamoyl-2,2-dimethyl-propyl)-amide
  参考文献：
  名称：

  Structure–activity relationships of the peptide deformylase inhibitor BB-3497: modification of the methylene spacer and the P1′ side chain

  摘要：

  Structural modifications to the peptide deformylase inhibitor BB-3497 are described. In this paper, we describe the initial SAR around this lead for modifications to the methylene spacer and the P1' side chain. Enzyme inhibition and antibacterial activity data revealed that the optimum distance between the N-formyl hydroxylamine metal binding group and the P1' side chain is one unsubstituted methylene unit. Additionally, lipophilic P1' side chains that closely mimic the methionine residue in the substrate provided compounds with the best microbiological profile. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(03)00532-8