N-(furan-2-yl)carbonyl-L-leucyl-L-phosphotryptophan diethyl ester | 219871-14-4

• 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: N-(furan-2-yl)carbonyl-L-leucyl-L-phosphotryptophan diethyl ester
• CAS: 219871-14-4
• 化学式: C₂₅H₃₄N₃O₆P
• 分子量: 503.535
• InChiKey: VYWIRIZMUZNGQI-JTHBVZDNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.86
• 重原子数：
  35.0
• 可旋转键数：
  13.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  122.66
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  N-(furan-2-yl)carbonyl-L-leucyl-L-phosphotryptophan diethyl ester 在 N,O-双三甲硅基乙酰胺 、 碘代三甲硅烷 作用下， 生成 [(R)-1-{(S)-2-[(Furan-2-carbonyl)-amino]-4-methyl-pentanoylamino}-2-(1H-indol-3-yl)-ethyl]-phosphonic acid
  参考文献：
  名称：

  Inhibition of Adamalysin II and MMPs by Phosphonate Analogues of Snake Venom Peptides

  摘要：

  Phosphonate analogues of the peptidomimetic N-(Furan-2-yl)carbonyl-Leu-Trp-OH were prepared with the goal of evaluating the effect of phosphonate for carboxylate replacement on binding with snake venom metalloproteinases and MMPs, N(Furan-2-yl)carbonyl-Leu-L-Trp(P)-(OH)(2) showed a 75-fold increase of the inhibiting activity against adamalysin II, a snake venom metalloproteinase structurally related to MMPs and TACE. Both the phosphonate and carboxylate peptidomimetics fit into the active site adopting a retrobinding mode and provide the structural base for a new class of metalloproteinases inhibitors. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(98)00243-0
• 作为产物：
  描述：

  L-亮氨酸甲酯盐酸盐 在 N-甲基吗啉 、 sodium hydroxide 、 氯甲酸异丁酯 作用下， 以 1,4-二氧六环 、 甲醇 为溶剂， 反应 31.0h， 生成 N-(furan-2-yl)carbonyl-L-leucyl-L-phosphotryptophan diethyl ester
  参考文献：
  名称：

  Inhibition of Adamalysin II and MMPs by Phosphonate Analogues of Snake Venom Peptides

  摘要：

  Phosphonate analogues of the peptidomimetic N-(Furan-2-yl)carbonyl-Leu-Trp-OH were prepared with the goal of evaluating the effect of phosphonate for carboxylate replacement on binding with snake venom metalloproteinases and MMPs, N(Furan-2-yl)carbonyl-Leu-L-Trp(P)-(OH)(2) showed a 75-fold increase of the inhibiting activity against adamalysin II, a snake venom metalloproteinase structurally related to MMPs and TACE. Both the phosphonate and carboxylate peptidomimetics fit into the active site adopting a retrobinding mode and provide the structural base for a new class of metalloproteinases inhibitors. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(98)00243-0