2-[2-[2-[2-[11-[11-[2-[2-[2-[2-(4-Methylphenyl)sulfonyloxyethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethyl 4-methylbenzenesulfonate | 1175039-12-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-[2-[2-[2-[11-[11-[2-[2-[2-[2-(4-Methylphenyl)sulfonyloxyethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethyl 4-methylbenzenesulfonate
• CAS: 1175039-12-9
• 化学式: C₅₂H₉₀O₁₄S₄
• 分子量: 1067.54
• InChiKey: VWTPGUVFGNBFQH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  10.7
• 重原子数：
  70
• 可旋转键数：
  53
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.77
• 拓扑面积：
  228
• 氢给体数：
  0
• 氢受体数：
  16

反应信息

• 作为反应物：
  描述：

  2-[2-[2-[2-[11-[11-[2-[2-[2-[2-(4-Methylphenyl)sulfonyloxyethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethyl 4-methylbenzenesulfonate 、 potassium phtalimide 以 N,N-二甲基甲酰胺 为溶剂， 反应 10.0h， 以60%的产率得到2-[2-[2-[2-[2-[11-[11-[2-[2-[2-[2-(1,3-Dioxoisoindol-2-yl)ethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethyl]isoindole-1,3-dione
  参考文献：
  名称：

  Selective Immobilization of Peptides Exclusively via N-Terminus Cysteines by Water-Driven Reactions on Surfaces

  摘要：

  Immobilizing peptides or proteins on bioinert surfaces enables the elucidation of ligand-receptor interaction in complex biological systems. Here, we report a highly chemoselective surface reaction that immobilizes peptides exclusively via N-terminus cysteine residue in a peptide. At pH 5.5, only N-terminus cysteines of peptides couple covalently with phenoxy amino squarate moieties presented oil self-assembled monolayers (SAMs) of alkailethiols oil gold Films. The selectivity of this surface reaction can tolerate the presence of internal cysteines in close proximity to basic residues such as histidines. We demonstrated this selective surface reaction by mammalian cell adhesion and by SAMDI mass spectroscopy of the SAMs.

  DOI：

  10.1021/jo901085u
• 作为产物：
  描述：

  2-[2-[2-[2-[11-[11-[2-[2-[2-(2-Hydroxyethoxy)ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethanol 、 对甲苯磺酰氯 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 以83%的产率得到2-[2-[2-[2-[11-[11-[2-[2-[2-[2-(4-Methylphenyl)sulfonyloxyethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethyl 4-methylbenzenesulfonate
  参考文献：
  名称：

  Selective Immobilization of Peptides Exclusively via N-Terminus Cysteines by Water-Driven Reactions on Surfaces

  摘要：

  Immobilizing peptides or proteins on bioinert surfaces enables the elucidation of ligand-receptor interaction in complex biological systems. Here, we report a highly chemoselective surface reaction that immobilizes peptides exclusively via N-terminus cysteine residue in a peptide. At pH 5.5, only N-terminus cysteines of peptides couple covalently with phenoxy amino squarate moieties presented oil self-assembled monolayers (SAMs) of alkailethiols oil gold Films. The selectivity of this surface reaction can tolerate the presence of internal cysteines in close proximity to basic residues such as histidines. We demonstrated this selective surface reaction by mammalian cell adhesion and by SAMDI mass spectroscopy of the SAMs.

  DOI：

  10.1021/jo901085u

文献信息

• Selective Immobilization of Peptides Exclusively via N-Terminus Cysteines by Water-Driven Reactions on Surfaces
  作者：Preeti Sejwal、Sri Kamesh Narasimhan、Deepali Prashar、Debjyoti Bandyopadhyay、Yan-Yeung Luk

  DOI：10.1021/jo901085u

  日期：2009.9.4

  Immobilizing peptides or proteins on bioinert surfaces enables the elucidation of ligand-receptor interaction in complex biological systems. Here, we report a highly chemoselective surface reaction that immobilizes peptides exclusively via N-terminus cysteine residue in a peptide. At pH 5.5, only N-terminus cysteines of peptides couple covalently with phenoxy amino squarate moieties presented oil self-assembled monolayers (SAMs) of alkailethiols oil gold Films. The selectivity of this surface reaction can tolerate the presence of internal cysteines in close proximity to basic residues such as histidines. We demonstrated this selective surface reaction by mammalian cell adhesion and by SAMDI mass spectroscopy of the SAMs.