(2R)-2-[1-[formyl(phenylmethoxy)amino]ethyl]hexanoic acid | 235786-21-7

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (2R)-2-[1-[formyl(phenylmethoxy)amino]ethyl]hexanoic acid
• CAS: 235786-21-7
• 化学式: C₁₆H₂₃NO₄
• 分子量: 293.363
• InChiKey: CYXGHNCSJTUPIN-AWKYBWMHSA-N

物化性质

• 沸点：
  434.755±55.00 °C(Press: 760.00 Torr)(predicted)
• 密度：
  1.126±0.06 g/cm3(Temp: 25 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  21
• 可旋转键数：
  9
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  66.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (2R)-2-[1-[formyl(phenylmethoxy)amino]ethyl]hexanoic acid 在 palladium on activated charcoal N-羟基-7-氮杂苯并三氮唑 、 氢气 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 生成 (R)-2-[1-(Formyl-hydroxy-amino)-ethyl]-hexanoic 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：

  (S)-4-苄基-3-己酰-2-恶唑烷酮 在 lithium hydroxide 、 双氧水 、 sodium acetate 、 sodium hexamethyldisilazane 、 sodium cyanoborohydride 作用下， 以 四氢呋喃 、 溶剂黄146 为溶剂， 生成 (2R)-2-[1-[formyl(phenylmethoxy)amino]ethyl]hexanoic acid
  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

文献信息

• US7323448B2
  申请人：——

  公开号：US7323448B2

  公开（公告）日：2008-01-29
• Structure–activity relationships of the peptide deformylase inhibitor BB-3497: modification of the methylene spacer and the P1′ side chain
  作者：Stephen J. Davies、Andrew P. Ayscough、R.Paul Beckett、Ryan A. Bragg、John M. Clements、Sheila Doel、Christine Grew、Steven B. Launchbury、Gemma M. Perkins、Lisa M. Pratt、Helen K. Smith、Zoë M. Spavold、S.Wayne Thomas、Richard S. Todd、Mark Whittaker

  DOI：10.1016/s0960-894x(03)00532-8

  日期：2003.8

  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.