3-[2-[2-[2-[2-[11-[11-[2-[2-[2-[2-[(3,4-Dioxo-2-phenoxycyclobuten-1-yl)amino]ethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethylamino]-4-phenoxycyclobut-3-ene-1,2-dione | 1175039-15-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3-[2-[2-[2-[2-[11-[11-[2-[2-[2-[2-[(3,4-Dioxo-2-phenoxycyclobuten-1-yl)amino]ethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethylamino]-4-phenoxycyclobut-3-ene-1,2-dione
• CAS: 1175039-15-2
• 化学式: C₅₈H₈₈N₂O₁₄S₂
• 分子量: 1101.47
• InChiKey: UQZLVONVUGULLA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  10.6
• 重原子数：
  76
• 可旋转键数：
  55
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.66
• 拓扑面积：
  235
• 氢给体数：
  2
• 氢受体数：
  18

反应信息

• 作为反应物：
  描述：

  3-[2-[2-[2-[2-[11-[11-[2-[2-[2-[2-[(3,4-Dioxo-2-phenoxycyclobuten-1-yl)amino]ethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethylamino]-4-phenoxycyclobut-3-ene-1,2-dione 、 c(RGDfK) 在 三乙胺 作用下， 以 二甲基亚砜 为溶剂， 以80%的产率得到
  参考文献：
  名称：

  Enhanced cell adhesion and mature intracellular structure promoted by squaramide-based RGD mimics on bioinert surfaces

  摘要：

  Highly selective molecular binding and the subsequent dynamic protein assemblies control the adhesion of mammalian cells. Molecules that inhibit cell adhesion have the therapeutic potential for a wide range of diseases. Here, we report an efficient synthesis (2-4 steps) of a class of squaramide molecules that mimics the natural tripeptide ligand Arg-Gly-Asp (RGD) that mediates mammalian cell adhesion through binding with membrane protein integrin. In solution, this class of squaramides exhibits a higher potency at inhibiting mammalian cell adhesion than RGD tripeptides. When immobilized on a bio-inert background formed by self-assembled monolayers of alkanethiols on gold films, squaramide ligands mediate vastly different intracellular structures than RGD ligands. Immunostaining revealed that the focal adhesions are smaller, but with a larger quantity, for cells adhered on squaramides than that on RGD ligands. Furthermore, the actin filaments are also more fibrous and well distributed for cell adhesion mediated by squaramide than that by RGD ligands. Quantification reveal that squaramide ligands mediate about 1.5 times more total focal adhesion (measured by the summation of the area of all focal adhesions) than that by natural RGD ligands. This result suggests that cell adhesion inhibitors, while blocking the attachment of cells to surfaces, may induce more focal adhesion proteins. Finally, this work demonstrates that immobilizing new ligands on bioinert surfaces provide a powerful tool to study mammalian cell adhesion. Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmc.2013.02.032
• 作为产物：
  描述：

  bis(23-amino-12,15,18,21-tetraoxatricosanyl)disulfide 、 3,4-di(phenoxy)cyclobut-3-ene-1,2-dione 以 四氢呋喃 为溶剂， 生成 3-[2-[2-[2-[2-[11-[11-[2-[2-[2-[2-[(3,4-Dioxo-2-phenoxycyclobuten-1-yl)amino]ethoxy]ethoxy]ethoxy]ethoxy]undecyldisulfanyl]undecoxy]ethoxy]ethoxy]ethoxy]ethylamino]-4-phenoxycyclobut-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