(9H-Fluoren-9-yl)methyl (R)-(2-(hydroxymethyl)-3-methylbutyl)carbamate | 1265892-38-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: (9H-Fluoren-9-yl)methyl (R)-(2-(hydroxymethyl)-3-methylbutyl)carbamate
• 英文别名: 9H-fluoren-9-ylmethyl N-[(2R)-2-(hydroxymethyl)-3-methylbutyl]carbamate
• CAS: 1265892-38-3
• 化学式: C₂₁H₂₅NO₃
• 分子量: 339.434
• InChiKey: LEQLCWCSWIDTCM-OAHLLOKOSA-N

物化性质

• 沸点：
  532.4±33.0 °C(Predicted)
• 密度：
  1.148±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.79
• 重原子数：
  25.0
• 可旋转键数：
  6.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  58.56
• 氢给体数：
  2.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  (9H-Fluoren-9-yl)methyl (R)-(2-(hydroxymethyl)-3-methylbutyl)carbamate 在 Jones reagent 作用下， 以 丙酮 为溶剂， 以172 mg的产率得到(R)-Fmoc-2-氨乙基-3-甲基丁酸盐酸盐
  参考文献：
  名称：

  Hairpin Folding Behavior of Mixed α/β-Peptides in Aqueous Solution

  摘要：

  The invention of new strategies for the design of protein-mimetic oligomers that manifest the folding encoded in natural amino acid sequences is a significant challenge. In contrast to the a-helix, mimicry of protein beta-sheets is less understood. We report here the aqueous folding behavior of a prototype alpha-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different beta-amino acid monomers. Our results provide a folding propensity scale for beta-residues in a protein beta-sheet context as well as high-resolution structures of several mixed-backbone alpha/beta-peptide hairpins in water.

  DOI：

  10.1021/ja2002346
• 作为产物：
  描述：

  在 palladium on carbon 、 甲酸铵 、 N,N-二异丙基乙胺 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 6.0h， 生成 (9H-Fluoren-9-yl)methyl (R)-(2-(hydroxymethyl)-3-methylbutyl)carbamate
  参考文献：
  名称：

  Hairpin Folding Behavior of Mixed α/β-Peptides in Aqueous Solution

  摘要：

  The invention of new strategies for the design of protein-mimetic oligomers that manifest the folding encoded in natural amino acid sequences is a significant challenge. In contrast to the a-helix, mimicry of protein beta-sheets is less understood. We report here the aqueous folding behavior of a prototype alpha-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different beta-amino acid monomers. Our results provide a folding propensity scale for beta-residues in a protein beta-sheet context as well as high-resolution structures of several mixed-backbone alpha/beta-peptide hairpins in water.

  DOI：

  10.1021/ja2002346