(S)-2-tert-Butoxycarbonylamino-3-(4-ethoxycarbonylmethoxy-phenyl)-propionic acid | 180078-11-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (S)-2-tert-Butoxycarbonylamino-3-(4-ethoxycarbonylmethoxy-phenyl)-propionic acid
• CAS: 180078-11-9
• 化学式: C₁₈H₂₅NO₇
• 分子量: 367.399
• InChiKey: HOOWKSXBYIBWLD-AWEZNQCLSA-N

物化性质

• 沸点：
  524.8±50.0 °C(Predicted)
• 密度：
  1.202±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.15
• 重原子数：
  26.0
• 可旋转键数：
  8.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  111.16
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (S)-2-tert-Butoxycarbonylamino-3-(4-ethoxycarbonylmethoxy-phenyl)-propionic acid 在 sodium hydroxide 、 三乙胺 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 生成 2-{4-[(2S)-2-{[(tert-butoxy)carbonyl]amino}-2-({4-[3-hydroxy-2-(methoxycarbonyl)phenoxy]butyl}carbamoyl)ethyl]phenoxy}acetic acid
  参考文献：
  名称：

  Discovery and SAR of novel, potent and selective protein tyrosine phosphatase 1B inhibitors

  摘要：

  A salicylate second site binder was linked to three classes of phosphotyrosine mimetics to produce potent protein tyrosine phosphatase 1B (PTP1B) inhibitors which exhibit significant selectivity against other phosphatases including the most homologous member, TCPTP.

  DOI：

  10.1016/s0960-894x(03)00725-x
• 作为产物：
  描述：

  丁氧羰基-酪氨酸-苄氧基酯 在 palladium on activated charcoal 氢气 、 potassium carbonate 作用下， 以 甲醇 、 乙腈 为溶剂， 生成 (S)-2-tert-Butoxycarbonylamino-3-(4-ethoxycarbonylmethoxy-phenyl)-propionic acid
  参考文献：
  名称：

  Identification of a monoacid-Based, cell permeable, selective inhibitor of protein tyrosine phosphatase 1B

  摘要：

  Monoacid-based PTP1B inhibitors with improved physiochemical properties have been investigated. A (2-hydroxy-phenoxy) acetic acid-based phosphotyrosyl mimetic has been linked with an optimized second arylphosphate binding site ligand to produce compound 20 with low micromolar potency against PTP1B, good selectivity over TCPTP (20-fold) and high cell permeability in the Caco-2 system.

  DOI：

  10.1016/j.bmcl.2003.08.064

文献信息

• Structure-activity relationships for macrocyclic peptidomimetic inhibitors of HIV-1 protease
  作者：G. Abbenante、D.A. Bergman、R.I. Brinkworth、D.R. March、R.C. Reid、P.A. Hunt、I.W. James、R.J. Dancer、B. Garnham、M.L. Stoermer、D.P. Fairlie

  DOI：10.1016/0960-894x(96)00468-4

  日期：1996.11

  A rational approach to developing inhibitors of proteolytic enzymes is the systematic modification of their peptide substrates to proteolytically stable, low molecular weight, nonpeptidic inhibitors. Replacing the scissile amide bond with a noncleavable transition state isostere usually gives potent protease inhibitors, but the remaining hydrolysable amide bonds render the inhibitors unstable to peptidases generally. Attempts to replace them with retention of inhibitor potency has proved difficult(1,2) due to the unpredictable cooperative influences of such variations on the conformations of both neighbouring inhibitor groups and enzyme residues. We recently described a method(3) for regioselectively fixing the conformation of inhibitor components and now show effects on activity of varying both the 'free' and 'fixed' components.