neopentyl 3-(5-acetylthiophen-2-yl)methanesulfonate | 446043-02-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并噻吩类
• 英文名称: neopentyl 3-(5-acetylthiophen-2-yl)methanesulfonate
• CAS: 446043-02-3
• 化学式: C₁₈H₂₀F₂O₄S₂
• 分子量: 402.483
• InChiKey: KGTXVNIFRYMVHA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.06
• 重原子数：
  26.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  60.44
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  neopentyl 3-(5-acetylthiophen-2-yl)methanesulfonate 在 potassium carbonate 、 碳酸氢铵 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 17.0h， 以98%的产率得到[3-(5'-acetylthiophen-2'-yl)phenyl]difluoromethanesulfonic acid ammonium salt
  参考文献：
  名称：

  The difluoromethylenesulfonic acid group as a monoanionic phosphate surrogate for obtaining PTP1B inhibitors

  摘要：

  Three peptides, 7-9, bearing sulfono(difluoromethyl)phenylalanine (F(2)Smp,2), a nonhydrolyzable, monoanionic phosphotyrosine mimetic, were prepared and evaluated as PTP1B inhibitors. The most effective inhibitor was the nonapeptide. ELEF(F(2)Smp)MDYE-NH2. (9) which exhibited a K-i of 360 nM. A comparison of F-2-Smp-bearing peptides 7 [DADE(F(2)Smp)LNH2. K-i=3.4 muM] and 8 [EEDE(F(2)Smp)LNH2. K-i=0.74 muM] with their phosphono(difluoromethyl)phenylalanine (F(2)Pmp)-bearing analogues indicated that F(2)Smp is not as effective a pTyr mimetic as F(2)Pmp by 100- to 130-fold. Although F(2)Smp is not as effective as F(2)Pmp, a comparison of peptide 7 with analagous peptides bearing other monoanionic pTyr mimetics recently reported in the literature indicates that F(2)Smp is about 65-fold more effective than any other non-hydrolyzable, monanionic pTyr mimetic reported to date. To further assess the difluoromethylenesulfonic acid (DFMS) group as a monoanionic phosphate mimetic, a series of 24 nonpeptidyl biaryl compounds bearing the DFMS group were prepared using polymer-supported methodologies and screened for PTP 1B inhibition. Several of these compounds were selected for further study and their IC50's compared to their difluoromethylenephosphonic (DFMP) analogues. The differences in IC50's between the DFMS and DFMP non-peptidyl compounds was not as great as with the F(2)Smp- and F(2)Pmp-bearing peptides. Possible reasons for this and its implication to the design of small molecule PTP1B inhibitors is discussed. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(02)00062-7
• 作为产物：
  描述：

  新戊醇 在 palladium diacetate 2,6-二甲基吡啶 、 水 、 sodium hexamethyldisilazane 、 potassium carbonate 、 N-氟代双苯磺酰胺 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 6.0h， 生成 neopentyl 3-(5-acetylthiophen-2-yl)methanesulfonate
  参考文献：
  名称：

  The difluoromethylenesulfonic acid group as a monoanionic phosphate surrogate for obtaining PTP1B inhibitors

  摘要：

  Three peptides, 7-9, bearing sulfono(difluoromethyl)phenylalanine (F(2)Smp,2), a nonhydrolyzable, monoanionic phosphotyrosine mimetic, were prepared and evaluated as PTP1B inhibitors. The most effective inhibitor was the nonapeptide. ELEF(F(2)Smp)MDYE-NH2. (9) which exhibited a K-i of 360 nM. A comparison of F-2-Smp-bearing peptides 7 [DADE(F(2)Smp)LNH2. K-i=3.4 muM] and 8 [EEDE(F(2)Smp)LNH2. K-i=0.74 muM] with their phosphono(difluoromethyl)phenylalanine (F(2)Pmp)-bearing analogues indicated that F(2)Smp is not as effective a pTyr mimetic as F(2)Pmp by 100- to 130-fold. Although F(2)Smp is not as effective as F(2)Pmp, a comparison of peptide 7 with analagous peptides bearing other monoanionic pTyr mimetics recently reported in the literature indicates that F(2)Smp is about 65-fold more effective than any other non-hydrolyzable, monanionic pTyr mimetic reported to date. To further assess the difluoromethylenesulfonic acid (DFMS) group as a monoanionic phosphate mimetic, a series of 24 nonpeptidyl biaryl compounds bearing the DFMS group were prepared using polymer-supported methodologies and screened for PTP 1B inhibition. Several of these compounds were selected for further study and their IC50's compared to their difluoromethylenephosphonic (DFMP) analogues. The differences in IC50's between the DFMS and DFMP non-peptidyl compounds was not as great as with the F(2)Smp- and F(2)Pmp-bearing peptides. Possible reasons for this and its implication to the design of small molecule PTP1B inhibitors is discussed. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(02)00062-7