methyl N-benzyl-N-(piperidin-4-yl)methioninate

• 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: methyl N-benzyl-N-(piperidin-4-yl)methioninate
• 英文别名: methyl (2S)-2-[benzyl(piperidin-4-yl)amino]-4-methylsulfanylbutanoate
• 化学式: C₁₈H₂₈N₂O₂S
• 分子量: 336.499
• InChiKey: HKMWJHGICDNVHN-KRWDZBQOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  23
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  66.9
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  4-氧代哌啶酮盐酸盐 在 盐酸 、 硼烷四氢呋喃络合物 、 3 A molecular sieve 、 sodium cyanoborohydride 、 三乙胺 、 N,N-二异丙基乙胺 作用下， 以 1,4-二氧六环 、 甲醇 、 二氯甲烷 、 水 为溶剂， 反应 136.0h， 生成 methyl N-benzyl-N-(piperidin-4-yl)methioninate
  参考文献：
  名称：

  Potent and Selective Farnesyl Transferase Inhibitors

  摘要：

  We recently described a novel series of CA(1)A(2)X peptidomimetics as farnesyl transferase inhibitors (FTIs). These compounds possess an N-(4-piperidinyl)benzamide scaffold mimicking A(1)A(2) residue. Extensive exploration of structure-activity relationships revealed that replacement of cysteine by substituted benzylimidazoles provided nanomolar FTIs with in vitro activities (18e, IC50 = 4.60 nM on isolated enzyme, EC50 = 20.0 nM for growth inhibition on a tumor cell line). The molecular docking of 18e and 19e in the active site of the enzyme provided details of key interactions with the protein and showed that the methionine or phenylalanine residue fits into the aryl binding site.

  DOI：

  10.1021/jm030502y

文献信息

• Potent and Selective Farnesyl Transferase Inhibitors
  作者：Régis Millet、Juozas Domarkas、Raymond Houssin、Pauline Gilleron、Jean-François Goossens、Philippe Chavatte、Cédric Logé,、Nicole Pommery、Jean Pommery、Jean-Pierre Hénichart

  DOI：10.1021/jm030502y

  日期：2004.12.1

  We recently described a novel series of CA(1)A(2)X peptidomimetics as farnesyl transferase inhibitors (FTIs). These compounds possess an N-(4-piperidinyl)benzamide scaffold mimicking A(1)A(2) residue. Extensive exploration of structure-activity relationships revealed that replacement of cysteine by substituted benzylimidazoles provided nanomolar FTIs with in vitro activities (18e, IC50 = 4.60 nM on isolated enzyme, EC50 = 20.0 nM for growth inhibition on a tumor cell line). The molecular docking of 18e and 19e in the active site of the enzyme provided details of key interactions with the protein and showed that the methionine or phenylalanine residue fits into the aryl binding site.