benzyl N-[2,2-dimethoxypropylcarbamoyl-[(4-hydroxy-3,5-diiodophenyl)methyl]amino]carbamate | 1025931-83-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: benzyl N-[2,2-dimethoxypropylcarbamoyl-[(4-hydroxy-3,5-diiodophenyl)methyl]amino]carbamate
• CAS: 1025931-83-2
• 化学式: C₂₁H₂₅I₂N₃O₆
• 分子量: 669.255
• InChiKey: HGQAFCFYLVMDSB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  32
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  109
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  benzyl N-[2,2-dimethoxypropylcarbamoyl-[(4-hydroxy-3,5-diiodophenyl)methyl]amino]carbamate 在 草酸 作用下， 以 四氢呋喃 为溶剂， 反应 12.0h， 生成 N-benzyloxycarbonyl-3,5-diiodo-α-azatyrosyl-1-aminopropan-2-one
  参考文献：
  名称：

  Peptidyl and azapeptidyl methylketones as substrate analog inhibitors of papain and cathepsin B

  摘要：

  Peptidyl methylketones containing Phe, Tyr, Tyr(I) Tyr(I-2), Leu and Ile in P-2 were synthesized and tested as substrate analog reversible inhibitors of papain and bovine spleen cathepsin B. The most effective cathepsin B inhibitor contained Tyr(I-2) and displayed an inhibition constant of 4.7 mu M at pH 6.8 and 25 degrees C, while Leu or lie gave practically inert analogs. Replacement of the amino acids in P-2 with the analogous alpha-azaamino acids, as well as the glycine in P-1 with alpha-azaglycine, led to complete loss of inhibiting activity. Introducing alkoxy substituents at the methyl adjacent to the ketone group generally resulted in more effective inhibitors, with inhibition constants in the micromolar range for both papain and cathepsin B.

  DOI：

  10.1016/0223-5234(96)88312-7
• 作为产物：
  描述：

  3,5-二碘-4-羟基苯甲醛 在 sodium cyanoborohydride 、 碳酸氢钠 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 氯仿 、 溶剂黄146 、 甲苯 为溶剂， 反应 23.0h， 生成 benzyl N-[2,2-dimethoxypropylcarbamoyl-[(4-hydroxy-3,5-diiodophenyl)methyl]amino]carbamate
  参考文献：
  名称：

  Peptidyl and azapeptidyl methylketones as substrate analog inhibitors of papain and cathepsin B

  摘要：

  Peptidyl methylketones containing Phe, Tyr, Tyr(I) Tyr(I-2), Leu and Ile in P-2 were synthesized and tested as substrate analog reversible inhibitors of papain and bovine spleen cathepsin B. The most effective cathepsin B inhibitor contained Tyr(I-2) and displayed an inhibition constant of 4.7 mu M at pH 6.8 and 25 degrees C, while Leu or lie gave practically inert analogs. Replacement of the amino acids in P-2 with the analogous alpha-azaamino acids, as well as the glycine in P-1 with alpha-azaglycine, led to complete loss of inhibiting activity. Introducing alkoxy substituents at the methyl adjacent to the ketone group generally resulted in more effective inhibitors, with inhibition constants in the micromolar range for both papain and cathepsin B.

  DOI：

  10.1016/0223-5234(96)88312-7