(R)-5-Methyl-3-((S)-1-phenyl-ethylcarbamoyl)-hexanoic acid methyl ester | 171347-91-4

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (R)-5-Methyl-3-((S)-1-phenyl-ethylcarbamoyl)-hexanoic acid methyl ester
• CAS: 171347-91-4
• 化学式: C₁₇H₂₅NO₃
• 分子量: 291.39
• InChiKey: YNFZENNGMPOAMU-DZGCQCFKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.09
• 重原子数：
  21.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  55.4
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  (R)-5-Methyl-3-((S)-1-phenyl-ethylcarbamoyl)-hexanoic acid methyl ester 在 盐酸 作用下， 以 氯仿 为溶剂， 以98%的产率得到(R)-2-(2-methoxy-2-oxoethyl)-4-methylpentanoic acid
  参考文献：
  名称：

  Matrix Metalloproteinase Inhibitors:  A Structure−Activity Study

  摘要：

  Modifications around the dipeptide-mimetic core of a hydroxamic acid based matrix metalloproteinase inhibitor were studied. These variations incorporated a variety of natural, unnatural, and synthetic amino acids in addition to modifications of the P1' and P3' substituents. The results of this study indicate the following structural requirements: (1) Two key hydrogen bonds must be present between the enzyme and potent substrates. (2) Potent inhibitors must possess strong zinc-binding functionalities. (3) The potential importance of the hydrophobic group at position R3 as illustrated by its ability to impart greater relative potency against stromelysin when larger hydrophobic groups are used. (4) Requirements surrounding the nature of the amino acid appear to be more restrictive for stromelysin than for neutrophil collagenase, 72 kDa gelatinase, and 92 kDa gelatinase. These requirements may involve planar fused-ring aryl systems and possibly hydrogen-bonding capabilities.

  DOI：

  10.1021/jm970494j
• 作为产物：
  描述：

  dihydro-3-(RS)-(2-methylpropyl)-2,5-furandione 以 乙醚 为溶剂， 反应 216.0h， 生成 (R)-5-Methyl-3-((S)-1-phenyl-ethylcarbamoyl)-hexanoic acid methyl ester
  参考文献：
  名称：

  Matrix Metalloproteinase Inhibitors:  A Structure−Activity Study

  摘要：

  Modifications around the dipeptide-mimetic core of a hydroxamic acid based matrix metalloproteinase inhibitor were studied. These variations incorporated a variety of natural, unnatural, and synthetic amino acids in addition to modifications of the P1' and P3' substituents. The results of this study indicate the following structural requirements: (1) Two key hydrogen bonds must be present between the enzyme and potent substrates. (2) Potent inhibitors must possess strong zinc-binding functionalities. (3) The potential importance of the hydrophobic group at position R3 as illustrated by its ability to impart greater relative potency against stromelysin when larger hydrophobic groups are used. (4) Requirements surrounding the nature of the amino acid appear to be more restrictive for stromelysin than for neutrophil collagenase, 72 kDa gelatinase, and 92 kDa gelatinase. These requirements may involve planar fused-ring aryl systems and possibly hydrogen-bonding capabilities.

  DOI：

  10.1021/jm970494j