(2S)-1-[(2R)-2-(benzylsulfonylamino)-4-oxo-4-(4-propan-2-ylpiperazin-1-yl)butanoyl]-N-[(4-carbamimidoylphenyl)methyl]pyrrolidine-2-carboxamide | 1321841-20-6

• 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: (2S)-1-[(2R)-2-(benzylsulfonylamino)-4-oxo-4-(4-propan-2-ylpiperazin-1-yl)butanoyl]-N-[(4-carbamimidoylphenyl)methyl]pyrrolidine-2-carboxamide
• CAS: 1321841-20-6
• 化学式: C₃₁H₄₃N₇O₅S
• 分子量: 625.792
• InChiKey: SUVKWOLSDPDTDN-SXOMAYOGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  44
• 可旋转键数：
  12
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.48
• 拓扑面积：
  177
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  BnSO2-D-Asp(OtBu)-Pro-NHBn(4-amidino) 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 反应 7.0h， 生成 (2S)-1-[(2R)-2-(benzylsulfonylamino)-4-oxo-4-(4-propan-2-ylpiperazin-1-yl)butanoyl]-N-[(4-carbamimidoylphenyl)methyl]pyrrolidine-2-carboxamide
  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

文献信息

• Development of substrate analogue inhibitors for the human airway trypsin-like protease HAT
  作者：Frank Sielaff、Eva Böttcher-Friebertshäuser、Daniela Meyer、Sebastian M. Saupe、Ines M. Volk、Wolfgang Garten、Torsten Steinmetzer

  DOI：10.1016/j.bmcl.2011.06.033

  日期：2011.8

  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.