3-Ethoxy-4-[2-[2-[2-[2-[11-[11-[2-[2-[2-[2-[(2-ethoxy-3,4-dioxocyclobuten-1-yl)amino]ethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethylamino]cyclobut-3-ene-1,2-dione | 1175039-14-1

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: 3-Ethoxy-4-[2-[2-[2-[2-[11-[11-[2-[2-[2-[2-[(2-ethoxy-3,4-dioxocyclobuten-1-yl)amino]ethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethylamino]cyclobut-3-ene-1,2-dione
• CAS: 1175039-14-1
• 化学式: C₅₀H₈₈N₂O₁₄S₂
• 分子量: 1005.39
• InChiKey: NAHLJLSEQQUMIQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.2
• 重原子数：
  68
• 可旋转键数：
  55
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.84
• 拓扑面积：
  235
• 氢给体数：
  2
• 氢受体数：
  18

反应信息

• 作为产物：
  描述：

  bis(23-amino-12,15,18,21-tetraoxatricosanyl)disulfide 、 方酸二乙酯 以 四氢呋喃 为溶剂， 生成 3-Ethoxy-4-[2-[2-[2-[2-[11-[11-[2-[2-[2-[2-[(2-ethoxy-3,4-dioxocyclobuten-1-yl)amino]ethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethylamino]cyclobut-3-ene-1,2-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

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.