| 219316-52-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• CAS: 219316-52-6
• 化学式: C₁₉H₁₆O₃
• 分子量: 292.334
• InChiKey: WDCYAEMBDZHNNM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.69
• 重原子数：
  22.0
• 可旋转键数：
  4.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  46.53
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  在 pyridinium chlorochromate 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 以95%的产率得到7-Formyl-naphthalene-2-carboxylic acid benzyl ester
  参考文献：
  名称：

  Structure-based design and synthesis of small molecule protein–tyrosine phosphatase 1B inhibitors

  摘要：

  Protein-tyrosine phosphatase (PTP) inhibitors are attractive as potential signal transduction-directed therapeutics which may be useful in the treatment of a variety of diseases. We have previously reported the X-ray structure of 1,1-difluoro-1-(2-naphthalenyl)methyl] phosphonic acid (4) complexed with the human the protein-tyrosine phosphatase 1B (PTP1B) and its use in the design of an analogue which binds with higher affinity within the catalytic site (Burke, T. R., Jr. et al. Biochemistry 1996, 35, 15989). In the current study, new naphthyldifluoromethyl phosphonic acids were designed bearing acidic functionality intended to interact with the PTP1B Arg47, which is situated just outside the catalytic pocket. This residue has been shown previously to provide key interactions with acidic residues of phosphotyrosyl-containing peptide substrates. Consistent with trends predicted by molecular dynamics calculations, the new analogues bound with 7- to 14-fold higher affinity than the parent 4, in principal validating the design rationale. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(98)00140-0
• 作为产物：
  描述：

  2,7-萘二羧酸二甲酯 在 4-二甲氨基吡啶 、 manganese(IV) oxide 、 sodium chlorite 、 potassium dihydrogenphosphate 、 lithium aluminium tetrahydride 、 2-甲基-2-丁烯 、 四丁基氟化铵 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 lithium hexamethyldisilazane 作用下， 以 四氢呋喃 、 水 、 N,N-二甲基甲酰胺 、 甲苯 、 叔丁醇 为溶剂， 反应 23.67h， 生成
  参考文献：
  名称：

  Structure-based design and synthesis of small molecule protein–tyrosine phosphatase 1B inhibitors

  摘要：

  Protein-tyrosine phosphatase (PTP) inhibitors are attractive as potential signal transduction-directed therapeutics which may be useful in the treatment of a variety of diseases. We have previously reported the X-ray structure of 1,1-difluoro-1-(2-naphthalenyl)methyl] phosphonic acid (4) complexed with the human the protein-tyrosine phosphatase 1B (PTP1B) and its use in the design of an analogue which binds with higher affinity within the catalytic site (Burke, T. R., Jr. et al. Biochemistry 1996, 35, 15989). In the current study, new naphthyldifluoromethyl phosphonic acids were designed bearing acidic functionality intended to interact with the PTP1B Arg47, which is situated just outside the catalytic pocket. This residue has been shown previously to provide key interactions with acidic residues of phosphotyrosyl-containing peptide substrates. Consistent with trends predicted by molecular dynamics calculations, the new analogues bound with 7- to 14-fold higher affinity than the parent 4, in principal validating the design rationale. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(98)00140-0