2-(3-phenyl-3-methylureido)benzoic acid | 352662-87-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-(3-phenyl-3-methylureido)benzoic acid
• 英文别名: 2-(3-methyl-3-phenylureido)benzoic acid；N-(methyl-phenyl-carbamoyl)-anthranilic acid；N-(Methyl-phenyl-carbamoyl)-anthranilsaeure；2-[[Methyl(phenyl)carbamoyl]amino]benzoic acid
• CAS: 352662-87-4
• 化学式: C₁₅H₁₄N₂O₃
• 分子量: 270.288
• InChiKey: DWCRYBNSASBTOR-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.4
• 重原子数：
  20
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  69.6
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-(3-phenyl-3-methylureido)benzoic acid 在 乙酸酐 作用下， 反应 0.25h， 以52%的产率得到2-methyl-phenyl-amino-4H-<3,1>-benzoxazin-4-one
  参考文献：
  名称：

  Inhibition of human chymase by 2-amino-3,1-benzoxazin-4-ones

  摘要：

  A series of 2-sec.amino-4H-3.1 -benzoxazin-4-ones was evaluated as acyl-enzyme inhibitors of human recombinant chymase. The compounds were also assayed for inhibition of human cathepsin G, bovine chemotrypsin, and human leukocyte elastase Introduction of an aromatic moiety into the 2-substituent resulted in strong inhibition of chymase. cathepsin G. and chymotrypsin. Extension of the N(Me)CH2Ph substituent by one methylene unit was unfavourable to inhibit these proteases Towards chymase, 2-(N-benzyl-N-methylamino)-4H-3, 1-benzoxazin-4-one (32) and 2-(N-benzyl-N-methylamino)-6-methyl-4H-3 1-benzoxazin-4-one (33) were found to exhibit K-i values of 11 and 17 nM, respectively, and form stable acyl-enzymes with half-lives of 53 and 25 min, respectively. Benzoxazinone 33 also inhibited the human chymase-catalyzed formation of angiotensin II from angiotensin I. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00310-2
• 作为产物：
  描述：

  靛红酸酐 、 N-甲基苯胺 以 乙醇 为溶剂， 反应 0.25h， 以42%的产率得到2-(3-phenyl-3-methylureido)benzoic acid
  参考文献：
  名称：

  Inhibition of human chymase by 2-amino-3,1-benzoxazin-4-ones

  摘要：

  A series of 2-sec.amino-4H-3.1 -benzoxazin-4-ones was evaluated as acyl-enzyme inhibitors of human recombinant chymase. The compounds were also assayed for inhibition of human cathepsin G, bovine chemotrypsin, and human leukocyte elastase Introduction of an aromatic moiety into the 2-substituent resulted in strong inhibition of chymase. cathepsin G. and chymotrypsin. Extension of the N(Me)CH2Ph substituent by one methylene unit was unfavourable to inhibit these proteases Towards chymase, 2-(N-benzyl-N-methylamino)-4H-3, 1-benzoxazin-4-one (32) and 2-(N-benzyl-N-methylamino)-6-methyl-4H-3 1-benzoxazin-4-one (33) were found to exhibit K-i values of 11 and 17 nM, respectively, and form stable acyl-enzymes with half-lives of 53 and 25 min, respectively. Benzoxazinone 33 also inhibited the human chymase-catalyzed formation of angiotensin II from angiotensin I. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00310-2

文献信息

• Aromatic 2-(Thio)ureidocarboxylic Acids As a New Family of Modulators of Multidrug Resistance-Associated Protein 1: Synthesis, Biological Evaluation, and Structure−Activity Relationships
  作者：Hans-Georg Häcker、Stefan Leyers、Jeanette Wiendlocha、Michael Gütschow、Michael Wiese

  DOI：10.1021/jm900688v

  日期：2009.8.13

  Four series of aromatic carboxylic acids were prepared with a urea or thiourea moiety at the neighboring position to the carboxyl group and benzene or thiophene as aromatic scaffold. Using a calcein AM assay, these compounds were evaluated as inhibitors of multidrug resistance-associated protein I (MRP1) and selected compounds were examined toward P-glycoprotein (P-gp) as well as breast cancer resistance protein (BCRP) to assess selectivity for MRP1. Two 2-thioureidobenzo[b]-thiophene-3-carboxylic acids (48, 49) were identified as particularly potent inhibitors of MRP1, with IC50 values of around 1 mu M. The structural features of this new family or nontoxic MRP1 inhibitors include a (thio)urea disubstituted with preferentially two alkyl groups at the terminal nitrogen and an additional fused aromatic ring.
• Inhibition of human chymase by 2-amino-3,1-benzoxazin-4-ones
  作者：Ulf Neumann、Norman M. Schechter、Michael Gütschow

  DOI：10.1016/s0968-0896(00)00310-2

  日期：2001.4

  A series of 2-sec.amino-4H-3.1 -benzoxazin-4-ones was evaluated as acyl-enzyme inhibitors of human recombinant chymase. The compounds were also assayed for inhibition of human cathepsin G, bovine chemotrypsin, and human leukocyte elastase Introduction of an aromatic moiety into the 2-substituent resulted in strong inhibition of chymase. cathepsin G. and chymotrypsin. Extension of the N(Me)CH2Ph substituent by one methylene unit was unfavourable to inhibit these proteases Towards chymase, 2-(N-benzyl-N-methylamino)-4H-3, 1-benzoxazin-4-one (32) and 2-(N-benzyl-N-methylamino)-6-methyl-4H-3 1-benzoxazin-4-one (33) were found to exhibit K-i values of 11 and 17 nM, respectively, and form stable acyl-enzymes with half-lives of 53 and 25 min, respectively. Benzoxazinone 33 also inhibited the human chymase-catalyzed formation of angiotensin II from angiotensin I. (C) 2001 Elsevier Science Ltd. All rights reserved.