(tert-butoxycarbonyl)-L-phenylalanyl-L-histidyl-(3S,4S)-statyl-L-leucine-10,11-dihydro-5H-methylenedibenzocycloheptenamide | 87691-46-1

• 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: (tert-butoxycarbonyl)-L-phenylalanyl-L-histidyl-(3S,4S)-statyl-L-leucine-10,11-dihydro-5H-methylenedibenzocycloheptenamide
• 英文别名: (tert-butoxycarbonyl)-L-phenylalanyl-L-histidyl-(3S,4S)-statyl-L-leucine-10,11-dihydro-5H-methylenedibenzo[a,d]cycloheptenamide；tert-butyl N-[(2S)-1-[[(2S)-1-[[(3S,4S)-3-hydroxy-6-methyl-1-[[(2S)-4-methyl-1-[(2-methylidene-9-tricyclo[9.4.0.03,8]pentadeca-1(15),3,5,7,11,13-hexaenyl)amino]-1-oxopentan-2-yl]amino]-1-oxoheptan-4-yl]amino]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]carbamate
• CAS: 87691-46-1
• 化学式: C₅₀H₆₅N₇O₇
• 分子量: 876.109
• InChiKey: JPVWOKQLLOKBLS-PAEKREDNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.86
• 重原子数：
  64.0
• 可旋转键数：
  19.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  203.64
• 氢给体数：
  7.0
• 氢受体数：
  8.0

反应信息

• 作为产物：
  描述：

  BOC-L-亮氨酸 在 盐酸 、 polystyrene-vinylbenzene resin 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 、 肼 、 亚硝酸异戊酯 作用下， 以 甲醇 为溶剂， 反应 15.25h， 生成 (tert-butoxycarbonyl)-L-phenylalanyl-L-histidyl-(3S,4S)-statyl-L-leucine-10,11-dihydro-5H-methylenedibenzocycloheptenamide
  参考文献：
  名称：

  Renin inhibitors. Statine-containing tetrapeptides with varied hydrophobic carboxy termini

  摘要：

  A series of statine-containing tetrapeptides, systematically modified at the carboxy terminus with various hydrophobic aromatic groups, is described. These compounds were tested in vitro for their ability to inhibit porcine, human plasma, and purified human kidney renins. These analogues help to define optimal binding aspects in a region of the enzyme that appears to be specific for spatial arrangement of aromatic groups. Replacement of the metabolically labile Phe amide with nonpeptidal groups proved possible while achieving inhibitory potency in the nanomolar range vs. porcine kidney renin. For the compounds 6i, 6m, and 6o, a large discrepancy in potency between the human plasma and the purified human kidney renin assays was observed. This disparity does not appear to be a consequence of a previously proposed plasma binding component.

  DOI：

  10.1021/jm00393a029