tetrahydro-3-(1-naphthalenyl)-(E)-6-<3-(trimethylsilyl)prop-2-ynylidene>-2H-pyran-2-one | 145475-83-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: tetrahydro-3-(1-naphthalenyl)-(E)-6-<3-(trimethylsilyl)prop-2-ynylidene>-2H-pyran-2-one
• 英文别名: (6E)-3-naphthalen-1-yl-6-(3-trimethylsilylprop-2-ynylidene)oxan-2-one
• CAS: 145475-83-8
• 化学式: C₂₁H₂₂O₂Si
• 分子量: 334.49
• InChiKey: PAIWQCNFSMOQRZ-LICLKQGHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.03
• 重原子数：
  24
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  tetrahydro-3-(1-naphthalenyl)-(E)-6-<3-(trimethylsilyl)prop-2-ynylidene>-2H-pyran-2-one 在 silver nitrate 作用下， 以 乙醇 为溶剂， 反应 1.0h， 以51%的产率得到tetrahydro-3-(1-naphthalenyl)-(E)-6-(prop-2-ynylidene)-2H-pyran-2-one
  参考文献：
  名称：

  Structural determinants of haloenol lactone-mediated suicide inhibition of canine myocardial calcium-independent phospholipase A2

  摘要：

  Haloenol lactones are potent mechanism im-based inhibitors of a novel class of calcium-independent phospholipases A2 Which have been implicated as the enzymic mediators of membrane dysfunction during myocardial ischemia (Hazen, S. L.; et al. J. Biol. Chem. 1991, 266,7227-7232). Herein we demonstrate that the ring size, hydrophobic group, and cryptic electrophile in the haloenol lactone moiety are important and modifiable determinants of the inhibitory potency of haloenol lactone-mediated inhibition of calcium-independent phospholipase A2. Direct comparisons between haloenol lactone-mediated inhibition of calcium-independent phospholipase A2 and the absence of inhibition with calcium-dependent phospholipase A2 further underscore the marked differences in the catalytic strategy employed by these two classes of intracellular phospholipases A2.

  DOI：

  10.1021/jm00053a012
• 作为产物：
  描述：

  2-(1-naphthyl)-5-hexynoic acid 在 bis(triphenylphosphine)palladium(II)-chloride 、 碘 、 potassium carbonate 、 三乙胺 、 copper(l) chloride 作用下， 以 乙腈 为溶剂， 反应 54.0h， 生成 tetrahydro-3-(1-naphthalenyl)-(E)-6-<3-(trimethylsilyl)prop-2-ynylidene>-2H-pyran-2-one
  参考文献：
  名称：

  Structural determinants of haloenol lactone-mediated suicide inhibition of canine myocardial calcium-independent phospholipase A2

  摘要：

  Haloenol lactones are potent mechanism im-based inhibitors of a novel class of calcium-independent phospholipases A2 Which have been implicated as the enzymic mediators of membrane dysfunction during myocardial ischemia (Hazen, S. L.; et al. J. Biol. Chem. 1991, 266,7227-7232). Herein we demonstrate that the ring size, hydrophobic group, and cryptic electrophile in the haloenol lactone moiety are important and modifiable determinants of the inhibitory potency of haloenol lactone-mediated inhibition of calcium-independent phospholipase A2. Direct comparisons between haloenol lactone-mediated inhibition of calcium-independent phospholipase A2 and the absence of inhibition with calcium-dependent phospholipase A2 further underscore the marked differences in the catalytic strategy employed by these two classes of intracellular phospholipases A2.

  DOI：

  10.1021/jm00053a012

文献信息

• Structural determinants of haloenol lactone-mediated suicide inhibition of canine myocardial calcium-independent phospholipase A2
  作者：Lori A. Zupan、Randy H. Weiss、Stanley L. Hazen、Barry L. Parnas、Karl W. Aston、Patrick J. Lennon、Daniel P. Getman、Richard W. Gross

  DOI：10.1021/jm00053a012

  日期：1993.1

  Haloenol lactones are potent mechanism im-based inhibitors of a novel class of calcium-independent phospholipases A2 Which have been implicated as the enzymic mediators of membrane dysfunction during myocardial ischemia (Hazen, S. L.; et al. J. Biol. Chem. 1991, 266,7227-7232). Herein we demonstrate that the ring size, hydrophobic group, and cryptic electrophile in the haloenol lactone moiety are important and modifiable determinants of the inhibitory potency of haloenol lactone-mediated inhibition of calcium-independent phospholipase A2. Direct comparisons between haloenol lactone-mediated inhibition of calcium-independent phospholipase A2 and the absence of inhibition with calcium-dependent phospholipase A2 further underscore the marked differences in the catalytic strategy employed by these two classes of intracellular phospholipases A2.