2,8-dibenzofuranbis(pentaflurophenyl 3-propionate) | 287957-58-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并呋喃
• 英文名称: 2,8-dibenzofuranbis(pentaflurophenyl 3-propionate)
• 英文别名: (2,3,4,5,6-Pentafluorophenyl) 3-[8-[3-oxo-3-(2,3,4,5,6-pentafluorophenoxy)propyl]dibenzofuran-2-yl]propanoate；(2,3,4,5,6-pentafluorophenyl) 3-[8-[3-oxo-3-(2,3,4,5,6-pentafluorophenoxy)propyl]dibenzofuran-2-yl]propanoate
• CAS: 287957-58-8
• 化学式: C₃₀H₁₄F₁₀O₅
• 分子量: 644.422
• InChiKey: DDPSFBQKDJIYBO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8
• 重原子数：
  45
• 可旋转键数：
  10
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.13
• 拓扑面积：
  65.7
• 氢给体数：
  0
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  2,8-dibenzofuranbis(pentaflurophenyl 3-propionate) 、 Val-Thr(bzl)-Val-Thr(bzl)-dmda bis(trifluoroacetate) 在 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 4.0h， 生成 Diac-(Val-Thr(bzl)-Val-Thr(bzl)-dmda)2
  参考文献：
  名称：

  Protofilaments, Filaments, Ribbons, and Fibrils from Peptidomimetic Self-Assembly:  Implications for Amyloid Fibril Formation and Materials Science

  摘要：

  Deciphering the mechanism(s) of beta-sheet mediated self-assembly is essential for understanding amyloid fibril formation and for the fabrication of polypeptide materials. Herein, we report a simple peptidomimetic that self-assembles into polymorphic beta-sheet quaternary structures including protofilaments, filaments, fibrils, and ribbons that are reminiscent of the highly ordered structures displayed by the amyloidogenic peptides A beta, calcitonin, and amylin. The distribution of quaternary structures can be controlled by and in some cases specified by manipulating the pH, buffer composition, and the ionic strength. The ability to control beta-sheet-mediated assembly takes advantage of quaternary structure dependent pK(a) perturbations. Biophysical methods including analytical ultracentrifugation studies as well as far-UV circular dichroism and FT-IR spectroscopy demonstrate that linked secondary and quaternary structural changes mediate peptidomimetic self-assembly. Electron and atomic force microscopy reveal that peptidomimetic assembly involves numerous quaternary structural intermediates that appear to self-assemble in a convergent fashion affording quaternary structures of increasing complexity. The ability to control the assembly pathway(s) and the final quaternary structure(s) afforded should prove to be particularly useful in deciphering the quaternary structural requirements for amyloid fibril formation and for the construction of noncovalent macromolecular structures.

  DOI：

  10.1021/ja9937831
• 作为产物：
  描述：

  二苯并呋喃 在 硫酸 sodium hydroxide 、 碘 、 palladium diacetate 、 碘酸 、 溶剂黄146 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 四氯化碳 、 乙醇 、 乙酸乙酯 、 N,N-二甲基甲酰胺 为溶剂， 98.0 ℃ 、310.26 kPa 条件下， 反应 32.5h， 生成 2,8-dibenzofuranbis(pentaflurophenyl 3-propionate)
  参考文献：
  名称：

  Protofilaments, Filaments, Ribbons, and Fibrils from Peptidomimetic Self-Assembly:  Implications for Amyloid Fibril Formation and Materials Science

  摘要：

  Deciphering the mechanism(s) of beta-sheet mediated self-assembly is essential for understanding amyloid fibril formation and for the fabrication of polypeptide materials. Herein, we report a simple peptidomimetic that self-assembles into polymorphic beta-sheet quaternary structures including protofilaments, filaments, fibrils, and ribbons that are reminiscent of the highly ordered structures displayed by the amyloidogenic peptides A beta, calcitonin, and amylin. The distribution of quaternary structures can be controlled by and in some cases specified by manipulating the pH, buffer composition, and the ionic strength. The ability to control beta-sheet-mediated assembly takes advantage of quaternary structure dependent pK(a) perturbations. Biophysical methods including analytical ultracentrifugation studies as well as far-UV circular dichroism and FT-IR spectroscopy demonstrate that linked secondary and quaternary structural changes mediate peptidomimetic self-assembly. Electron and atomic force microscopy reveal that peptidomimetic assembly involves numerous quaternary structural intermediates that appear to self-assemble in a convergent fashion affording quaternary structures of increasing complexity. The ability to control the assembly pathway(s) and the final quaternary structure(s) afforded should prove to be particularly useful in deciphering the quaternary structural requirements for amyloid fibril formation and for the construction of noncovalent macromolecular structures.

  DOI：

  10.1021/ja9937831

文献信息

• Protofilaments, Filaments, Ribbons, and Fibrils from Peptidomimetic Self-Assembly:  Implications for Amyloid Fibril Formation and Materials Science
  作者：Hilal A. Lashuel、Steven R. LaBrenz、Linda Woo、Louise C. Serpell、Jeffery W. Kelly

  DOI：10.1021/ja9937831

  日期：2000.6.1

  Deciphering the mechanism(s) of beta-sheet mediated self-assembly is essential for understanding amyloid fibril formation and for the fabrication of polypeptide materials. Herein, we report a simple peptidomimetic that self-assembles into polymorphic beta-sheet quaternary structures including protofilaments, filaments, fibrils, and ribbons that are reminiscent of the highly ordered structures displayed by the amyloidogenic peptides A beta, calcitonin, and amylin. The distribution of quaternary structures can be controlled by and in some cases specified by manipulating the pH, buffer composition, and the ionic strength. The ability to control beta-sheet-mediated assembly takes advantage of quaternary structure dependent pK(a) perturbations. Biophysical methods including analytical ultracentrifugation studies as well as far-UV circular dichroism and FT-IR spectroscopy demonstrate that linked secondary and quaternary structural changes mediate peptidomimetic self-assembly. Electron and atomic force microscopy reveal that peptidomimetic assembly involves numerous quaternary structural intermediates that appear to self-assemble in a convergent fashion affording quaternary structures of increasing complexity. The ability to control the assembly pathway(s) and the final quaternary structure(s) afforded should prove to be particularly useful in deciphering the quaternary structural requirements for amyloid fibril formation and for the construction of noncovalent macromolecular structures.