(2S,3R,4S)-2-({[(dimethylamino)carbonyl]-L-phenylalanyl-L-histidyl}amino)-1-cyclohexyl-3,4-dihydroxy-6-methylheptane | 114457-18-0

• 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,3R,4S)-2-({[(dimethylamino)carbonyl]-L-phenylalanyl-L-histidyl}amino)-1-cyclohexyl-3,4-dihydroxy-6-methylheptane
• 英文别名: N-[1-(1-Cyclohexylmethyl-2,3-dihydroxy-5-methyl-hexylcarbamoyl)-2-(1H-imidazol-4-yl)-ethyl]-2-(3,3-dimethyl-ureido)-3-phenyl-propionamide；(2S)-N-[(2S)-1-[[(2S,3R,4S)-1-cyclohexyl-3,4-dihydroxy-6-methylheptan-2-yl]amino]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]-2-(dimethylcarbamoylamino)-3-phenylpropanamide
• CAS: 114457-18-0
• 化学式: C₃₂H₅₀N₆O₅
• 分子量: 598.786
• InChiKey: BUTLRPLOHRQFSC-MYHRABSESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  43
• 可旋转键数：
  15
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  160
• 氢给体数：
  6
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  (S)-2-异氰酰基-3-苯基丙酸 在 lithium hydroxide 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 15.67h， 生成 (2S,3R,4S)-2-({[(dimethylamino)carbonyl]-L-phenylalanyl-L-histidyl}amino)-1-cyclohexyl-3,4-dihydroxy-6-methylheptane
  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

文献信息

• Renin inhibitors. Dipeptide analogs of angiotensinogen utilizing a structurally modified phenylalanine residue to impart proteolytic stability
  作者：Jacob J. Plattner、Patrick A. Marcotte、Hollis D. Kleinert、Herman H. Stein、Jonathan Greer、Giorgio Bolis、Anthony K. L. Fung、Barbara A. Bopp、Jay R. Luly

  DOI：10.1021/jm00120a006

  日期：1988.12

  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.