3-(N-fluorenylmethoxycarbonylamino)-4-cyano benzylbutyrate | 247217-27-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: 3-(N-fluorenylmethoxycarbonylamino)-4-cyano benzylbutyrate
• CAS: 247217-27-2
• 化学式: C₂₇H₂₄N₂O₄
• 分子量: 440.499
• InChiKey: DXKUOXJNOCFJKY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.94
• 重原子数：
  33.0
• 可旋转键数：
  8.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.22
• 拓扑面积：
  88.42
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  3-(N-fluorenylmethoxycarbonylamino)-4-cyano benzylbutyrate 在 盐酸 、 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 水 为溶剂， 反应 6.0h， 生成 (S)-2-[3-(9H-Fluoren-9-ylmethoxycarbonylamino)-4-((S)-1-methoxycarbonyl-2-phenyl-ethylcarbamoyl)-butyrylamino]-3-phenyl-propionic acid methyl ester
  参考文献：
  名称：

  Synthesis and conformation of dipeptide taste ligands containinghomo-β-amino acid residues

  摘要：

  The synthesis and conformational properties of a series of dipeptide taste ligands, differing from the commercial sweetener aspartame by the presence of a methylene group between the C-alpha and the C' carbon atoms (as in homo-beta-residues) in either the L-Asp or the L-Phe residues, are described. Homo-beta-residues such as homo-beta-aspartic acid, homo-beta-phenylglycine and homo-beta-phenylalanine, obtained by homologation of the corresponding proteinogenic alpha-amino acids, have been used in the solution peptide synthesis of the following aspartame analogues in protected and unprotected forms: NH2-homo-beta-(L or D)-Asp-L-Phe-OMe, NH2-L-Asp-homo-beta-L-Phg-OMe and NH2-L-Asp-homo-beta-L-Phe-OMe. Lengthening of the peptide skeleton at the L-Asp site results in a drastic loss of sweetness with the production of tasteless compounds; on the other hand, lengthening of the skeleton at the C-terminal L-Phe site partially mantains the sweet taste in both NH2-L-Asp-homo-beta-L-Phe-OMe and NH2-L-Asp-homo-beta-L-Phg-OMe. The solution conformation of the synthesized dipeptide taste ligands was investigated by NMR and circular dichroism techniques. The analysis of NMR data combined with restrained molecular dynamics calculations shows that all peptides are fairly flexible and they do not assume a preferred conformation in DMSO and methanol. The peptides containing homo-beta-L-Phe and homo-beta-L-Phg do adopt a discrete number of conformations among which mainly extended and 'L-shaped' conformation are represented. The circular dichroism spectra are consistent with the NMR results, indicating a significant flexibility for these compounds. Copyright (C) 1999 John Wiley & Sons, Ltd.

  DOI：

  10.1002/(sici)1099-1395(199907)12:7<577::aid-poc159>3.0.co;2-f
• 作为产物：
  描述：

  3-(N-tert-butyloxycarbonylamino)-4-cyano benzylbutyrate 在 sodium carbonate 、 三氟乙酸 作用下， 以 四氢呋喃 、 二氯甲烷 、 水 为溶剂， 反应 2.5h， 生成 3-(N-fluorenylmethoxycarbonylamino)-4-cyano benzylbutyrate
  参考文献：
  名称：

  Synthesis and conformation of dipeptide taste ligands containinghomo-β-amino acid residues

  摘要：

  The synthesis and conformational properties of a series of dipeptide taste ligands, differing from the commercial sweetener aspartame by the presence of a methylene group between the C-alpha and the C' carbon atoms (as in homo-beta-residues) in either the L-Asp or the L-Phe residues, are described. Homo-beta-residues such as homo-beta-aspartic acid, homo-beta-phenylglycine and homo-beta-phenylalanine, obtained by homologation of the corresponding proteinogenic alpha-amino acids, have been used in the solution peptide synthesis of the following aspartame analogues in protected and unprotected forms: NH2-homo-beta-(L or D)-Asp-L-Phe-OMe, NH2-L-Asp-homo-beta-L-Phg-OMe and NH2-L-Asp-homo-beta-L-Phe-OMe. Lengthening of the peptide skeleton at the L-Asp site results in a drastic loss of sweetness with the production of tasteless compounds; on the other hand, lengthening of the skeleton at the C-terminal L-Phe site partially mantains the sweet taste in both NH2-L-Asp-homo-beta-L-Phe-OMe and NH2-L-Asp-homo-beta-L-Phg-OMe. The solution conformation of the synthesized dipeptide taste ligands was investigated by NMR and circular dichroism techniques. The analysis of NMR data combined with restrained molecular dynamics calculations shows that all peptides are fairly flexible and they do not assume a preferred conformation in DMSO and methanol. The peptides containing homo-beta-L-Phe and homo-beta-L-Phg do adopt a discrete number of conformations among which mainly extended and 'L-shaped' conformation are represented. The circular dichroism spectra are consistent with the NMR results, indicating a significant flexibility for these compounds. Copyright (C) 1999 John Wiley & Sons, Ltd.

  DOI：

  10.1002/(sici)1099-1395(199907)12:7<577::aid-poc159>3.0.co;2-f