((R)-3-Methyl-1-propyl-butyl)-carbamic acid tert-butyl ester | 129603-09-4

• 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: ((R)-3-Methyl-1-propyl-butyl)-carbamic acid tert-butyl ester
• 英文别名: tert-butyl N-[(4R)-2-methylheptan-4-yl]carbamate
• CAS: 129603-09-4
• 化学式: C₁₃H₂₇NO₂
• 分子量: 229.363
• InChiKey: VUBLXMCFOBUIFA-LLVKDONJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.73
• 重原子数：
  16.0
• 可旋转键数：
  5.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  38.33
• 氢给体数：
  1.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  ((R)-3-Methyl-1-propyl-butyl)-carbamic acid tert-butyl ester 在 N-甲基吗啉 、 盐酸 、 氯甲酸异丁酯 作用下， 以 乙酸乙酯 为溶剂， 反应 20.25h， 生成
  参考文献：
  名称：

  Gastrin releasing peptide antagonists with improved potency and stability

  摘要：

  Gastrin releasing peptide (GRP) is a 27 amino acid peptide hormone which is homologous to the amphibian peptide bombesin. Two series of novel GRP antagonists were developed by C-terminal modification of N-acetyl-GRP-20-27 amide. Peptide derivatives within each series resist enzymatic degradation in serum and exhibit strong affinity for the GRP receptor. The first series of compounds replaces the Leu26-Met27 region of GRP with an alkyl ether moiety. One member of this series, N-acetyl-GRP-20-25-NH-[(S)-1-ethoxy-4-methyl-2-pentane], specifically blocked radiolabeled GRP binding with an IC50 of 6 nM. In the second series of antagonists the oxygen of the ether moiety is replaced with a methylene group, resulting in GRP antagonists which are equipotent to native GRP in receptor binding assays (IC50 = 2 nM) and are also resistant to proteolytic degradation in vitro. All of the C-terminally modified peptides tested blocked GRP-stimulated mitogenesis in Swiss 3T3 mouse fibroblasts. Representative compounds also blocked GRP-induced elevation of [Ca2+]i in human SCLC cells, and inhibited GRP-independent release of gastrin in vivo.

  DOI：

  10.1021/jm00111a027
• 作为产物：
  描述：

  ((Z)-(S)-1-Isobutyl-but-2-enyl)-carbamic acid tert-butyl ester 在 palladium catalyst 氢气 作用下， 以 乙醇 为溶剂， 生成 ((R)-3-Methyl-1-propyl-butyl)-carbamic acid tert-butyl ester
  参考文献：
  名称：

  Gastrin releasing peptide antagonists with improved potency and stability

  摘要：

  Gastrin releasing peptide (GRP) is a 27 amino acid peptide hormone which is homologous to the amphibian peptide bombesin. Two series of novel GRP antagonists were developed by C-terminal modification of N-acetyl-GRP-20-27 amide. Peptide derivatives within each series resist enzymatic degradation in serum and exhibit strong affinity for the GRP receptor. The first series of compounds replaces the Leu26-Met27 region of GRP with an alkyl ether moiety. One member of this series, N-acetyl-GRP-20-25-NH-[(S)-1-ethoxy-4-methyl-2-pentane], specifically blocked radiolabeled GRP binding with an IC50 of 6 nM. In the second series of antagonists the oxygen of the ether moiety is replaced with a methylene group, resulting in GRP antagonists which are equipotent to native GRP in receptor binding assays (IC50 = 2 nM) and are also resistant to proteolytic degradation in vitro. All of the C-terminally modified peptides tested blocked GRP-stimulated mitogenesis in Swiss 3T3 mouse fibroblasts. Representative compounds also blocked GRP-induced elevation of [Ca2+]i in human SCLC cells, and inhibited GRP-independent release of gastrin in vivo.

  DOI：

  10.1021/jm00111a027

文献信息

• A Convenient and Versatile Synthesis of Chiral Aliphatic and Allylic Amines
  作者：Walfred S. Saari、Thorsten E. Fisher

  DOI：10.1055/s-1990-26900

  日期：——

  Preparation of optically pure aliphatic and allylic amines from amino acids is described. Wittig olefination of α-Boc-amino aldehydes affords Boc-protected allylic amines which can be deprotected to the corresponding chiral unsaturated amines. Catalytic reduction of the Wittig product prior to deprotection affords aliphatic amines of high optical purity.

  本文描述了从氨基酸制备光学纯脂肪族和烯丙基胺的方法。通过Wittig烯烃化反应，将α-Boc-氨基酸醛转化为Boc保护的烯丙基胺，再脱保护得到相应的手性不饱和胺。在脱保护之前对Wittig产物进行催化还原，可以获得高光学纯度的脂肪族胺。
• SAARI, WALFRED S.;FISHER, THORSTEN E., LAB. MICROCOMPUT., 9,(1990) N, C. 453-454
  作者：SAARI, WALFRED S.、FISHER, THORSTEN E.

  DOI：——

  日期：——