11-[2-(2-Methoxyethoxy)ethoxy]undec-1-ene | 219641-36-8

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 11-[2-(2-Methoxyethoxy)ethoxy]undec-1-ene
• CAS: 219641-36-8
• 化学式: C₁₆H₃₂O₃
• 分子量: 272.428
• InChiKey: CRNCWLDIFBJJSF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.3
• 重原子数：
  19
• 可旋转键数：
  16
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  27.7
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  11-[2-(2-Methoxyethoxy)ethoxy]undec-1-ene 在 盐酸 、 偶氮二异丁腈 、 乙二胺四乙酸 作用下， 以 甲醇 为溶剂， 生成 2,5,8-trioxanonadecane-19-thiol
  参考文献：
  名称：

  Factors that Determine the Protein Resistance of Oligoether Self-Assembled Monolayers − Internal Hydrophilicity, Terminal Hydrophilicity, and Lateral Packing Density

  摘要：

  Protein resistance of oligoether self-assembled monolayers (SAMS) on gold and silver surfaces has been investigated systematically to elucidate structural factors that determine whether a SAM will be able to resist protein adsorption. Oligo(ethylene glycol) (OEG)-, oligo(propylene glycol)-, and oligo(trimethylene glycol)-terminated alkanethiols with different chain lengths and alkyl termination were synthesized as monolayer constituents. The packing density and chemical composition of the SAMS were examined by XPS spectroscopy; the terminal hydrophilicity was characterized by contact angle measurements. IRRAS spectroscopy gave information about the chain conformation of specific monolayers; the amount of adsorbed protein as compared to alkanethiol monolayers was determined by ellipsometry. We found several factors that in combination or by themselves suppress the protein resistance of oligoether monolayers. Monolayers with a hydrophobic interior, such as those containing oligo(propylene glycol), show no protein resistance. The lateral compression of oligo(ethylene glycol) monolayers on silver generates more highly ordered monolayers and may cause decreased protein resistance, but does not necessarily lead to an all-trans chain conformation of the OEG moieties. Water contact angles higher than 70degrees on gold or 65degrees on silver reduce full protein resistance. We conclude that both internal and terminal hydrophilicity favor the protein resistance of an oligoether monolayer. It is suggested that the penetration of water molecules in the interior of the SAM is a necessary prerequisite for protein resistance. We discuss and summarize the various factors which are critical for the functionality of "inert" organic films.

  DOI：

  10.1021/ja034820y
• 作为产物：
  描述：

  11-溴-1-十一烯 在 sodium hydride 作用下， 以 四氢呋喃 为溶剂， 生成 11-[2-(2-Methoxyethoxy)ethoxy]undec-1-ene
  参考文献：
  名称：

  Factors that Determine the Protein Resistance of Oligoether Self-Assembled Monolayers − Internal Hydrophilicity, Terminal Hydrophilicity, and Lateral Packing Density

  摘要：

  Protein resistance of oligoether self-assembled monolayers (SAMS) on gold and silver surfaces has been investigated systematically to elucidate structural factors that determine whether a SAM will be able to resist protein adsorption. Oligo(ethylene glycol) (OEG)-, oligo(propylene glycol)-, and oligo(trimethylene glycol)-terminated alkanethiols with different chain lengths and alkyl termination were synthesized as monolayer constituents. The packing density and chemical composition of the SAMS were examined by XPS spectroscopy; the terminal hydrophilicity was characterized by contact angle measurements. IRRAS spectroscopy gave information about the chain conformation of specific monolayers; the amount of adsorbed protein as compared to alkanethiol monolayers was determined by ellipsometry. We found several factors that in combination or by themselves suppress the protein resistance of oligoether monolayers. Monolayers with a hydrophobic interior, such as those containing oligo(propylene glycol), show no protein resistance. The lateral compression of oligo(ethylene glycol) monolayers on silver generates more highly ordered monolayers and may cause decreased protein resistance, but does not necessarily lead to an all-trans chain conformation of the OEG moieties. Water contact angles higher than 70degrees on gold or 65degrees on silver reduce full protein resistance. We conclude that both internal and terminal hydrophilicity favor the protein resistance of an oligoether monolayer. It is suggested that the penetration of water molecules in the interior of the SAM is a necessary prerequisite for protein resistance. We discuss and summarize the various factors which are critical for the functionality of "inert" organic films.

  DOI：

  10.1021/ja034820y