tert-butyl N-[(2R)-1-[[(2S,3S)-1-(2,4-dimethylanilino)-3-methyl-1-oxopentan-2-yl]amino]-3-tritylsulfanylpropan-2-yl]carbamate | 1026386-11-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: tert-butyl N-[(2R)-1-[[(2S,3S)-1-(2,4-dimethylanilino)-3-methyl-1-oxopentan-2-yl]amino]-3-tritylsulfanylpropan-2-yl]carbamate
• CAS: 1026386-11-7
• 化学式: C₄₁H₅₁N₃O₃S
• 分子量: 665.94
• InChiKey: FRMDFUOPLAHJSM-QIMHXLKXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.2
• 重原子数：
  48
• 可旋转键数：
  16
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  105
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  tert-butyl N-[(2R)-1-[[(2S,3S)-1-(2,4-dimethylanilino)-3-methyl-1-oxopentan-2-yl]amino]-3-tritylsulfanylpropan-2-yl]carbamate 在 三乙基硅烷 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 生成 (2S,3S)-2-[[(2R)-2-amino-3-[[(2R)-2-amino-3-[[(2S,3S)-1-(2,4-dimethylanilino)-3-methyl-1-oxopentan-2-yl]amino]propyl]disulfanyl]propyl]amino]-N-(2,4-dimethylphenyl)-3-methylpentanamide
  参考文献：
  名称：

  Pseudodipeptide Inhibitors of Protein Farnesyltransferase

  摘要：

  A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase). These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed protein farnesylation. In contrast to CAAX peptidomimetics previously reported, these inhibitors do not have a C-terminal carboxyl moiety, yet they inhibit farnesylation in vitro at <100 nM. Despite the absence of the X residue in the CAAX motif, which normally directs prenylation specificity, these pseudodipeptides are greater than 100-fold selective for PFTase over type 1 protein geranylgeranyltransferase.

  DOI：

  10.1021/jm00020a010
• 作为产物：
  描述：

  L-异亮氨酸 在 3 A molecular sieve 、 双(2-氧代-3-恶唑烷基)次磷酰氯 、 sodium cyanoborohydride 、 N,N-二异丙基乙胺 作用下， 以 乙醇 、 二氯甲烷 为溶剂， 反应 20.0h， 生成 tert-butyl N-[(2R)-1-[[(2S,3S)-1-(2,4-dimethylanilino)-3-methyl-1-oxopentan-2-yl]amino]-3-tritylsulfanylpropan-2-yl]carbamate
  参考文献：
  名称：

  Pseudodipeptide Inhibitors of Protein Farnesyltransferase

  摘要：

  A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase). These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed protein farnesylation. In contrast to CAAX peptidomimetics previously reported, these inhibitors do not have a C-terminal carboxyl moiety, yet they inhibit farnesylation in vitro at <100 nM. Despite the absence of the X residue in the CAAX motif, which normally directs prenylation specificity, these pseudodipeptides are greater than 100-fold selective for PFTase over type 1 protein geranylgeranyltransferase.

  DOI：

  10.1021/jm00020a010

文献信息

• Pseudodipeptide Inhibitors of Protein Farnesyltransferase
  作者：S. Jane deSolms、Albert A. Deana、Elizabeth A. Giuliani、Samuel L. Graham、Nancy E. Kohl、Scott D. Mosser、Allen I. Oliff、David L. Pompliano、Elaine Rands

  DOI：10.1021/jm00020a010

  日期：1995.9

  A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase). These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed protein farnesylation. In contrast to CAAX peptidomimetics previously reported, these inhibitors do not have a C-terminal carboxyl moiety, yet they inhibit farnesylation in vitro at <100 nM. Despite the absence of the X residue in the CAAX motif, which normally directs prenylation specificity, these pseudodipeptides are greater than 100-fold selective for PFTase over type 1 protein geranylgeranyltransferase.