bis(23-amino-12,15,18,21-tetraoxatricosanyl)disulfide | 1160998-98-0

• 分子结构分类: 有机化合物 - 有机硫化合物 - 有机二硫化物
• 英文名称: bis(23-amino-12,15,18,21-tetraoxatricosanyl)disulfide
• 英文别名: 2-[2-[2-[2-[11-[11-[2-[2-[2-(2-Aminoethoxy)ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethanamine
• CAS: 1160998-98-0
• 化学式: C₃₈H₈₀N₂O₈S₂
• 分子量: 757.194
• InChiKey: WQPNYLIOJHHKNG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.1
• 重原子数：
  50
• 可旋转键数：
  47
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  177
• 氢给体数：
  2
• 氢受体数：
  12

反应信息

• 作为反应物：
  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
• 作为产物：
  描述：

  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 在 一水合肼 作用下， 以 乙醇 为溶剂， 反应 12.0h， 生成 bis(23-amino-12,15,18,21-tetraoxatricosanyl)disulfide
  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

• Gold-Ferrocene Glyco-Nanoparticles for High-Sensitivity Electrochemical Detection of Carbohydrate-Lectin Interactions
  作者：Manuel C. Martos-Maldonado、Mikkel B. Thygesen、Knud J. Jensen、Antonio Vargas-Berenguel

  DOI：10.1002/ejoc.201300205

  日期：2013.5

  mannose-binding lectin concanavalin A by both optical and electrochemical methods, based on the surface-plasmon-resonance (SPR)-shift properties of the metal and the electrochemical activity of the ferrocene moiety, respectively. Moreover, they could be used to detect concanavalin A with high sensitivity in the low nanomolar range by electrochemical methods. A comparison of their redox-sensing abilities

  本文报道了用甘露糖-二茂铁缀合物包覆的两种水溶性金纳米粒子的方便制备。该制备涉及使用不对称的 1,1'-双取代二茂铁结构单元，允许它们与炔丙基 α-D-吡喃甘露糖苷和二硫化物官能化接头连续正交偶联，用于将甘露糖-二茂铁共轭物锚定到金属表面。纳米粒子的不同之处在于接头与二茂铁环戊二烯基环的结合方式：通过酰胺键或三唑基甲基。虽然前者在水中在光照下不稳定，但在黑暗中稳定，后者在两种情况下都稳定。基于金属的表面等离子体共振 (SPR) 位移特性和二茂铁部分的电化学活性，甘露糖-二茂铁涂覆的金纳米粒子通过光学和电化学方法对甘露糖结合凝集素刀豆蛋白 A 表现出传感能力， 分别。此外，它们可用于通过电化学方法在低纳摩尔范围内以高灵敏度检测伴刀豆球蛋白 A。将它们的氧化还原传感能力与单价和二价甘露糖-二茂铁偶联物的氧化还原传感能力进行比较表明，甘露糖和二茂铁单元的多价呈现导致灵敏度显着提高，检测限至少为三
• 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.