BnSO2-D-Asp-Pro-NHBn(4-amidino) | 1321841-04-6

• 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: BnSO2-D-Asp-Pro-NHBn(4-amidino)
• 英文别名: (3R)-3-(benzylsulfonylamino)-4-[(2S)-2-[(4-carbamimidoylphenyl)methylcarbamoyl]pyrrolidin-1-yl]-4-oxobutanoic acid
• CAS: 1321841-04-6
• 化学式: C₂₄H₂₉N₅O₆S
• 分子量: 515.59
• InChiKey: XPWOFOOTIJPQSH-UXHICEINSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  36
• 可旋转键数：
  11
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  191
• 氢给体数：
  5
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  苄基-1-哌嗪碳酸酯 、 BnSO2-D-Asp-Pro-NHBn(4-amidino) 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 反应 6.0h， 生成 benzyl 4-[(3R)-3-(benzylsulfonylamino)-4-[(2S)-2-[(4-carbamimidoylphenyl)methylcarbamoyl]pyrrolidin-1-yl]-4-oxobutanoyl]piperazine-1-carboxylate
  参考文献：
  名称：

  Development of substrate analogue inhibitors for the human airway trypsin-like protease HAT

  摘要：

  A series of substrate analogue inhibitors of the serine protease HAT, containing a 4-amidinobenzylamide moiety as the P1 residue, was prepared. The most potent compounds possess a basic amino acid in the D-configuration as P3 residue. Whereas inhibitor 4 (K-i 13 nM) containing proline as the P2 residue completely lacks selectivity, incorporation of norvaline leads to a potent inhibitor (15, K-i 15 nM) with improved selectivity for HAT in comparison to the coagulation proteases thrombin and factor Xa or the fibrinolytic plasmin. Selected inhibitors were able to suppress influenza virus replication in a HAT-expressing MDCK cell model. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.06.033
• 作为产物：
  描述：

  BnSO2-D-Asp(OtBu)-Pro-NHBn(4-amidino) 在 三氟乙酸 作用下， 反应 1.0h， 生成 BnSO2-D-Asp-Pro-NHBn(4-amidino)
  参考文献：
  名称：

  Development of substrate analogue inhibitors for the human airway trypsin-like protease HAT

  摘要：

  A series of substrate analogue inhibitors of the serine protease HAT, containing a 4-amidinobenzylamide moiety as the P1 residue, was prepared. The most potent compounds possess a basic amino acid in the D-configuration as P3 residue. Whereas inhibitor 4 (K-i 13 nM) containing proline as the P2 residue completely lacks selectivity, incorporation of norvaline leads to a potent inhibitor (15, K-i 15 nM) with improved selectivity for HAT in comparison to the coagulation proteases thrombin and factor Xa or the fibrinolytic plasmin. Selected inhibitors were able to suppress influenza virus replication in a HAT-expressing MDCK cell model. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.06.033