(2S,4S)-4-amino-2-tert-butyldimethylsiloxymethyl-3-oxo-6-methyl-1,2-oxiranylheptane | 214753-31-8

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (2S,4S)-4-amino-2-tert-butyldimethylsiloxymethyl-3-oxo-6-methyl-1,2-oxiranylheptane
• CAS: 214753-31-8
• 化学式: C₁₅H₃₁NO₃Si
• 分子量: 301.502
• InChiKey: BXCGRWMPEQDGOS-WFASDCNBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.72
• 重原子数：
  20.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.93
• 拓扑面积：
  64.85
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  (2S,4S)-4-amino-2-tert-butyldimethylsiloxymethyl-3-oxo-6-methyl-1,2-oxiranylheptane 在 四丁基氟化铵 、 N,N-二异丙基乙胺 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 11.0h， 生成 Dihydroeponemycin
  参考文献：
  名称：

  Eponemycin analogues: syntheses and use as probes of angiogenesis

  摘要：

  Derivatives of the epoxy-beta-aminoketone containing natural product eponemycin have been prepared in order to study the molecular mode of action of this anti-angiogenic compound. Synthesis and use of a biotinylated dihydroeponemycin analogue demonstrated that dihydroeponemycin forms a covalent adduct with at least two intracellular proteins in human endothelial cells. Pretreatment of cells with a five equivalent excess of dihydroeponemycin precluded biotin-dihydroeponemycin binding indicating a specific interaction between natural product and the target proteins. This biotin-dihydroeponemycin derivative will prove useful in the purification and identification of eponemycin receptors. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(98)00089-3
• 作为产物：
  描述：

  (3RS,4S)-4-benzyloxycarbonylamino-2-tert-butyldimethylsiloxymethyl-3-hydroxy-6-methyl-1-heptene 在 palladium on activated charcoal 草酰氯 、 氢气 、 双氧水 、 二甲基亚砜 、 三乙胺 、 N,N-二异丙基乙胺 作用下， 以 甲醇 、 二氯甲烷 、 苯甲腈 为溶剂， 反应 15.0h， 生成 (2S,4S)-4-amino-2-tert-butyldimethylsiloxymethyl-3-oxo-6-methyl-1,2-oxiranylheptane
  参考文献：
  名称：

  Eponemycin analogues: syntheses and use as probes of angiogenesis

  摘要：

  Derivatives of the epoxy-beta-aminoketone containing natural product eponemycin have been prepared in order to study the molecular mode of action of this anti-angiogenic compound. Synthesis and use of a biotinylated dihydroeponemycin analogue demonstrated that dihydroeponemycin forms a covalent adduct with at least two intracellular proteins in human endothelial cells. Pretreatment of cells with a five equivalent excess of dihydroeponemycin precluded biotin-dihydroeponemycin binding indicating a specific interaction between natural product and the target proteins. This biotin-dihydroeponemycin derivative will prove useful in the purification and identification of eponemycin receptors. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(98)00089-3

文献信息

• Total synthesis of (+)-epopromycin B and its analogues—studies on the inhibition of cellulose biosynthesis
  作者：Markus R Dobler

  DOI：10.1016/s0040-4039(00)01944-4

  日期：2001.1

  The described inhibition of the cellulose biosynthesis by epopromycin B prompted us to establish a short and efficient synthesis of the natural product, suitable for accessing a broad range of unnatural analogues in a multiparallel fashion. During the course of our synthesis the absolute configuration of (+)-epopromycin B could be determined. (C) 2000 Elsevier Science Ltd. All rights reserved.
• A bright approach to the immunoproteasome: Development of LMP2/β1i-specific imaging probes
  作者：Kimberly Cornish Carmony、Do-Min Lee、Ying Wu、Na-Ra Lee、Marie Wehenkel、Jason Lee、Beilei Lei、Chang-Guo Zhan、Kyung-Bo Kim

  DOI：10.1016/j.bmc.2011.06.039

  日期：2012.1

  While the constitutive, 26S proteasome plays an important role in regulating many important cellular processes, a variant form known as the immunoproteasome is thought to primarily function in adaptive immune responses. However, recent studies indicate an association of immunoproteasomes with many physiological disorders such as cancer, neurodegenerative, and inflammatory diseases. Despite this, the detailed functions of the immunoproteasome remain poorly understood. Immunoproteasome-specific probes are essential to gain insight into immunoproteasome function. Here, we describe for the first time the development of cell-permeable activity-based fluorescent probes, UK101-Fluor and UK101-B660, which selectively target the catalytically active LMP2/beta 1i subunit of the immunoproteasome. These probes facilitate rapid detection of the cellular localization of catalytically active immunoproteasomes in living cells, providing a valuable tool to analyze immunoproteasome functions. Additionally, as LMP2/beta 1i may serve as a potential tumor biomarker, an LMP2/beta 1i-targeting fluorescent imaging probe may be applicable to a rapid readout assay to determine tumor LMP2/beta 1i levels. (C) 2011 Elsevier Ltd. All rights reserved.