d-Hexafluorpropanol-2 | 38701-72-3

• 分子结构分类: 有机化合物 - 有机卤素化合物 - 卤代醇
• 英文名称: d-Hexafluorpropanol-2
• 英文别名: 1,1,1,3,3,3-Hexafluoro-2-propanol-d(1)；2-deuterio-1,1,1,3,3,3-hexafluoro-propan-2-ol；2-Deuterio-1,1,1,3,3,3-hexafluoropropan-2-ol
• CAS: 38701-72-3
• 化学式: C₃H₂F₆O
• 分子量: 169.031
• InChiKey: BYEAHWXPCBROCE-MICDWDOJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  10
• 可旋转键数：
  0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  20.2
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  1,1,1,3,3,3-六氟代-2-氘代丙醇 在 水 作用下， 生成 d-Hexafluorpropanol-2
  参考文献：
  名称：

  NMR Study of Interactions between Silk Model Peptide and Fluorinated Alcohols for Preparation of Regenerated Silk Fiber

  摘要：

  The fluorinated organic solvents 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) and hexafluoro-acetone trihydrate (HFA) have been successfully used to produce silk fibroin Fibers with high strength. To understand the reasons for the difference in strength between regenerated silk fibers prepared from these two solvents, we analyzed and compared properties of the native silk fibroin and (AGSGAG)(2), a model for the crystalline part of fibroin, in the two solvents. The C-13 and H-1 chemical shifts obtained from H-1-C-13 HSQC spectra of silk fibroin in HFIP, HFA, and water indicates that silk fibroin formed helix-like structure in the fluorinated alcohols. A similar tendency was observed for (AGSGAG)(2) although the chemical shift change is smaller. Intramolecular H-1-H-1 NOE data for (AGSGAG)(2) imply the presence of helical structures in the middle part of the peptide in HFIP and bill not in HFA, although all equilibrating collection of conformations likely are present in both solvents. For the peptide dissolved in HFIP, cross-relaxation parameters (sigma(HF)) arising from interactions between spins of the solvent and the solute are in good agreement for most protons of the peptide with those predicted from theory. In contrast, observed sigma(HF) for peptide in HFA are negative at all residues while positive sigma(HF) are expected. These results are interpreted to indicate that solute-solvent interactions in HFA persist longer than in HFIP.

  DOI：

  10.1021/ma902544c
• 作为试剂：
  描述：

  环戊酸 在 氘代乙腈 、 d-Hexafluorpropanol-2 、 sodium 2,2,2-trifluoroacetate 、 palladium diacetate 、 6-(quinuclidin-2-ylmethyl)pyridin-2-ol 、 silver carbonate 作用下， 以24 %的产率得到
  参考文献：
  名称：

  通过配体脱氢合成 β,γ-不饱和脂肪酸

  摘要：

  脂肪酸的α,β-脱氢是通过烯醇化和β-C-H金属化途径实现的。然而，迄今为止，通过脱氢合成分离的β,γ-不饱和脂肪酸尚未实现。在此，我们报道了丰富且廉价的游离脂肪酸的配体启用的β，γ-脱氢，这提供了一种新的合成断开以及复杂分子在远程γ位点的下游功能化的通用平台。各种游离脂肪酸，包括环尺寸从五元到大环的无环和环状系统，都可以进行有效的脱氢。值得注意的是，该方案在存在更容易接近的 α-C-H 键的情况下具有良好的化学选择性，并且在融合双环支架中具有出色的区域选择性。该协议的实用性已通过一系列生物活性萜烯天然产物在 γ 位点的后期功能化得到证明。 β,γ-双键的进一步功能化允许将共价弹头（包括环氧化物、氮丙啶和β-内酯）安装到复杂的天然产物支架中，这对于靶向共价药物的发现很有价值。

  DOI：

  10.1021/jacs.3c06423

文献信息

• NMR Study of Interactions between Silk Model Peptide and Fluorinated Alcohols for Preparation of Regenerated Silk Fiber
  作者：Yu Suzuki、J. T. Gerig、Tetsuo Asakura

  DOI：10.1021/ma902544c

  日期：2010.3.9

  The fluorinated organic solvents 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) and hexafluoro-acetone trihydrate (HFA) have been successfully used to produce silk fibroin Fibers with high strength. To understand the reasons for the difference in strength between regenerated silk fibers prepared from these two solvents, we analyzed and compared properties of the native silk fibroin and (AGSGAG)(2), a model for the crystalline part of fibroin, in the two solvents. The C-13 and H-1 chemical shifts obtained from H-1-C-13 HSQC spectra of silk fibroin in HFIP, HFA, and water indicates that silk fibroin formed helix-like structure in the fluorinated alcohols. A similar tendency was observed for (AGSGAG)(2) although the chemical shift change is smaller. Intramolecular H-1-H-1 NOE data for (AGSGAG)(2) imply the presence of helical structures in the middle part of the peptide in HFIP and bill not in HFA, although all equilibrating collection of conformations likely are present in both solvents. For the peptide dissolved in HFIP, cross-relaxation parameters (sigma(HF)) arising from interactions between spins of the solvent and the solute are in good agreement for most protons of the peptide with those predicted from theory. In contrast, observed sigma(HF) for peptide in HFA are negative at all residues while positive sigma(HF) are expected. These results are interpreted to indicate that solute-solvent interactions in HFA persist longer than in HFIP.