7-[[Tert-butyl(dimethyl)silyl]oxymethyl]naphthalene-2-carbaldehyde | 219316-49-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 7-[[Tert-butyl(dimethyl)silyl]oxymethyl]naphthalene-2-carbaldehyde
• 英文别名: 7-[[tert-butyl(dimethyl)silyl]oxymethyl]naphthalene-2-carbaldehyde
• CAS: 219316-49-1
• 化学式: C₁₈H₂₄O₂Si
• 分子量: 300.473
• InChiKey: RLQCOYNQQZCWIW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.17
• 重原子数：
  21
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 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：

  7-[[Tert-butyl(dimethyl)silyl]oxymethyl]naphthalene-2-carbaldehyde 在 sodium chlorite 、 potassium dihydrogenphosphate 、 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 、 pyridinium chlorochromate 作用下， 以 四氢呋喃 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 、 叔丁醇 为溶剂， 反应 22.0h， 生成 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-萘双(三氟甲磺酸酯) 在 4-二甲氨基吡啶 、 manganese(IV) oxide 、 palladium diacetate 、 lithium aluminium tetrahydride 、 1,3-双(二苯基膦)丙烷 、 三乙胺 、 lithium hexamethyldisilazane 作用下， 以 四氢呋喃 、 二甲基亚砜 、 甲苯 为溶剂， 反应 8.67h， 生成 7-[[Tert-butyl(dimethyl)silyl]oxymethyl]naphthalene-2-carbaldehyde
  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

文献信息

• Enzymatic Approach to Unnatural Glycosides with Diverse Aglycon Scaffolds Using Glycosyltransferase VinC
  作者：Atsushi Minami、Rei Uchida、Tadashi Eguchi、Katsumi Kakinuma

  DOI：10.1021/ja042848j

  日期：2005.5.1

  Glycosyltransferase VinC was explored for a construction of glycoside libraries using dTDP-vicenisamine and structurally unrelated unnatural aglycons, and new unnatural vicenisaminides were successfully constructed. Structural elements of aglycon recognition by VinC were proposed by modeling studies and were confirmed by the success of transglycosylation upon a designed aglycon.
• Structure-based design and synthesis of small molecule protein–tyrosine phosphatase 1B inhibitors
  作者：Zhu-Jun Yao、Bin Ye、Xiong-Wu Wu、Shaomeng Wang、Li Wu、Zhong-Yin Zhang、Terrence R. Burke

  DOI：10.1016/s0968-0896(98)00140-0

  日期：1998.10

  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.