(R)-6-Azido-3-tert-butoxycarbonylamino-5-(tert-butyl-dimethyl-silanyloxy)-hexanoic acid | 540721-23-1

• 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: (R)-6-Azido-3-tert-butoxycarbonylamino-5-(tert-butyl-dimethyl-silanyloxy)-hexanoic acid
• 英文别名: (3R)-6-azido-5-[tert-butyl(dimethyl)silyl]oxy-3-[(2-methylpropan-2-yl)oxycarbonylamino]hexanoic acid
• CAS: 540721-23-1
• 化学式: C₁₇H₃₄N₄O₅Si
• 分子量: 402.566
• InChiKey: IGCDUNGFTLVPCU-PZORYLMUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.45
• 重原子数：
  27
• 可旋转键数：
  12
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  99.2
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  (R)-6-Azido-3-tert-butoxycarbonylamino-5-(tert-butyl-dimethyl-silanyloxy)-hexanoic acid 在 吡啶 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 32.0h， 生成
  参考文献：
  名称：

  N- and C-terminal modifications of negamycin

  摘要：

  Negamycin 1 is a bactericidal antibiotic with activity against Gram-negative bacteria, and served as a template in an antibiotic discovery program. An orthogonally protected beta-amino acid derivative 3a was synthesized and used in parallel synthesis of negamycin derivatives on solid support. This advanced intermediate was also used for N- and C-terminal modifications using solution-phase methodologies. The N-terminal modifications have resulted in the identification of active analogues, whereas the C-terminal modifications resulted in complete loss of antibacterial activity. The N-methyl negamycin analogue, 19a, inhibits protein synthesis (IC50 = 2.3 muM), has antibacterial activity (Escherichia coli, MIC = 16 mug/mL), and is efficacious in an E. coli murine septicemia model (ED50 = 16.3 mg/kg). (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(03)00393-7
• 作为产物：
  描述：

  ((R)-2-Iodomethyl-6-oxo-tetrahydro-pyran-4-yl)-carbamic acid tert-butyl ester 在 咪唑 、 lithium hydroxide 、 sodium azide 、 potassium carbonate 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 26.0h， 生成 (R)-6-Azido-3-tert-butoxycarbonylamino-5-(tert-butyl-dimethyl-silanyloxy)-hexanoic acid
  参考文献：
  名称：

  N- and C-terminal modifications of negamycin

  摘要：

  Negamycin 1 is a bactericidal antibiotic with activity against Gram-negative bacteria, and served as a template in an antibiotic discovery program. An orthogonally protected beta-amino acid derivative 3a was synthesized and used in parallel synthesis of negamycin derivatives on solid support. This advanced intermediate was also used for N- and C-terminal modifications using solution-phase methodologies. The N-terminal modifications have resulted in the identification of active analogues, whereas the C-terminal modifications resulted in complete loss of antibacterial activity. The N-methyl negamycin analogue, 19a, inhibits protein synthesis (IC50 = 2.3 muM), has antibacterial activity (Escherichia coli, MIC = 16 mug/mL), and is efficacious in an E. coli murine septicemia model (ED50 = 16.3 mg/kg). (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(03)00393-7

文献信息

• N- and C-terminal modifications of negamycin
  作者：B Raju、Kathleen Mortell、Sampathkumar Anandan、Hardwin O'Dowd、Hongwu Gao、Marcela Gomez、Corinne Hackbarth、Charlotte Wu、Wen Wang、Zhengyu Yuan、Richard White、Joaquim Trias、Dinesh V Patel

  DOI：10.1016/s0960-894x(03)00393-7

  日期：2003.7

  Negamycin 1 is a bactericidal antibiotic with activity against Gram-negative bacteria, and served as a template in an antibiotic discovery program. An orthogonally protected beta-amino acid derivative 3a was synthesized and used in parallel synthesis of negamycin derivatives on solid support. This advanced intermediate was also used for N- and C-terminal modifications using solution-phase methodologies. The N-terminal modifications have resulted in the identification of active analogues, whereas the C-terminal modifications resulted in complete loss of antibacterial activity. The N-methyl negamycin analogue, 19a, inhibits protein synthesis (IC50 = 2.3 muM), has antibacterial activity (Escherichia coli, MIC = 16 mug/mL), and is efficacious in an E. coli murine septicemia model (ED50 = 16.3 mg/kg). (C) 2003 Elsevier Science Ltd. All rights reserved.