N-(2-ethoxy-3,4-dioxocyclobut-1-en-1-yl)-S-trityl-L-cysteine | 1429121-47-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: N-(2-ethoxy-3,4-dioxocyclobut-1-en-1-yl)-S-trityl-L-cysteine
• CAS: 1429121-47-0
• 化学式: C₂₈H₂₅NO₅S
• 分子量: 487.576
• InChiKey: YTMLUILGLXMRPO-QFIPXVFZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.27
• 重原子数：
  35.0
• 可旋转键数：
  11.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  92.7
• 氢给体数：
  2.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  N-(2-ethoxy-3,4-dioxocyclobut-1-en-1-yl)-S-trityl-L-cysteine 、 4, 4'-ethylenedipiperidine dihydrochloride 在 三乙胺 作用下， 以 乙醇 为溶剂， 反应 12.0h， 以60%的产率得到N-[2-(4-(2-(piperidin-4-yl)ethyl)piperidin-1-yl)-3,4-dioxo-1-cyclobuten-1-yl]-S-trityl-L-cysteine
  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：

  S-三苯甲基-L-半胱氨酸 、 方酸二乙酯 在 4-二甲氨基吡啶 、 三乙胺 作用下， 以 水 为溶剂， 反应 3.0h， 以85%的产率得到N-(2-ethoxy-3,4-dioxocyclobut-1-en-1-yl)-S-trityl-L-cysteine
  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