(4-Benzyl-benzyl)-[2-((S)-2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-4-methyl-pentyl]-phosphinic acid methyl ester | 202975-49-3

• 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: (4-Benzyl-benzyl)-[2-((S)-2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-4-methyl-pentyl]-phosphinic acid methyl ester
• CAS: 202975-49-3
• 化学式: C₂₉H₄₃N₂O₄P
• 分子量: 514.645
• InChiKey: PCJFCLHEFJPIFA-IMHIQEPFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.64
• 重原子数：
  36.0
• 可旋转键数：
  12.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  84.5
• 氢给体数：
  2.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  (4-Benzyl-benzyl)-[2-((S)-2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-4-methyl-pentyl]-phosphinic acid methyl ester 在 水 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 18.0h， 生成 S,S (4-benzylbenzyl)[2-(2,2-dimethyl-1-methylcarbamoyl propylcarbamoyl)4-methylpentyl]phosphinic acid
  参考文献：
  名称：

  Inhibition of MMP-1 and MMP-13 with phosphinic acids that exploit binding in the S2 pocket

  摘要：

  Through the use of empirical and computational methods, phosphinate-based inhibitors of MMP-1 and MMP-13 that bind into the S-2 pocket of these enzymes were designed. The synthesis and testing of 2 suggested that binding was occurring as hypothesized. Structure determination of a co-crystal of 2 bound to the catalytic domain of MMP-1 confirmed the binding mode. Substituents binding into S-2, S-1', S-2' and S-3', were optimized yielding compounds with low double-digit nM IC50's against these enzymes. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(98)00729-x
• 作为产物：
  描述：

  [(RS)-2-[(benzyloxy)carbonyl]-4-methylpentyl]phosphinic acid 在 palladium on barium sulfate N,O-双三甲硅基乙酰胺 、 氢气 、 (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 甲醇 、 乙醇 、 二氯甲烷 、 甲苯 为溶剂， 反应 19.5h， 生成 (4-Benzyl-benzyl)-[2-((S)-2,2-dimethyl-1-methylcarbamoyl-propylcarbamoyl)-4-methyl-pentyl]-phosphinic acid methyl ester
  参考文献：
  名称：

  Inhibition of MMP-1 and MMP-13 with phosphinic acids that exploit binding in the S2 pocket

  摘要：

  Through the use of empirical and computational methods, phosphinate-based inhibitors of MMP-1 and MMP-13 that bind into the S-2 pocket of these enzymes were designed. The synthesis and testing of 2 suggested that binding was occurring as hypothesized. Structure determination of a co-crystal of 2 bound to the catalytic domain of MMP-1 confirmed the binding mode. Substituents binding into S-2, S-1', S-2' and S-3', were optimized yielding compounds with low double-digit nM IC50's against these enzymes. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(98)00729-x