(4-morpholinylcarbonyl)-L-homophenylalanine | 116129-73-8

• 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: (4-morpholinylcarbonyl)-L-homophenylalanine
• 英文别名: (2S)-2-(morpholine-4-carbonylamino)-4-phenylbutanoic acid
• CAS: 116129-73-8
• 化学式: C₁₅H₂₀N₂O₄
• 分子量: 292.335
• InChiKey: NWCQAOJNWPCZLY-ZDUSSCGKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  21
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  78.9
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (4-morpholinylcarbonyl)-L-homophenylalanine 、 (S)-2-Amino-N-((1S,2R,3S)-1-cyclohexylmethyl-2,3-dihydroxy-5-methyl-hexyl)-3-(1H-imidazol-4-yl)-propionamide; hydrochloride 在 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以63%的产率得到Morpholine-4-carboxylic acid {(S)-1-[(S)-1-((1S,2R,3S)-1-cyclohexylmethyl-2,3-dihydroxy-5-methyl-hexylcarbamoyl)-2-(1H-imidazol-4-yl)-ethylcarbamoyl]-3-phenyl-propyl}-amide
  参考文献：
  名称：

  Renin inhibitors. Dipeptide analogs of angiotensinogen utilizing a structurally modified phenylalanine residue to impart proteolytic stability

  摘要：

  A series of renin inhibitors have been prepared and evaluated for their susceptibility to cleavage by the serine protease chymotrypsin. The compounds were designed by consideration of the structural requirements in the active-site region of renin and chymotrypsin. By systematic alteration of the P3 phenylalanine residue, compounds with varying degrees of renin inhibitory potency and chymotrypsin susceptibility were obtained. Selected analogues from this group were examined in vivo for both their hypotensive effects and metabolic patterns.

  DOI：

  10.1021/jm00120a006
• 作为产物：
  描述：

  (alphaS)-alpha-氨基苯丁酸甲酯盐酸盐 在 lithium hydroxide 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 水 、 甲苯 为溶剂， 反应 1.17h， 生成 (4-morpholinylcarbonyl)-L-homophenylalanine
  参考文献：
  名称：

  Renin inhibitors. Dipeptide analogs of angiotensinogen utilizing a structurally modified phenylalanine residue to impart proteolytic stability

  摘要：

  A series of renin inhibitors have been prepared and evaluated for their susceptibility to cleavage by the serine protease chymotrypsin. The compounds were designed by consideration of the structural requirements in the active-site region of renin and chymotrypsin. By systematic alteration of the P3 phenylalanine residue, compounds with varying degrees of renin inhibitory potency and chymotrypsin susceptibility were obtained. Selected analogues from this group were examined in vivo for both their hypotensive effects and metabolic patterns.

  DOI：

  10.1021/jm00120a006