2-Oxo-3-<2-carboxy-ethyl>-tetrahydrofuran | 936-83-4

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 英文名称: 2-Oxo-3-<2-carboxy-ethyl>-tetrahydrofuran
• 英文别名: 3-(2-Carboxy-ethyl)-2-oxo-tetrahydrofuran；3-(2-oxo-tetrahydro-furan-3-yl)-propionic acid；3-(2-oxo-tetrahydro-[3]furyl)-propionic acid；3-(2-Oxo-tetrahydro-[3]furyl)-propionsaeure；3-(2-Oxooxolan-3-yl)propanoic acid
• CAS: 936-83-4
• 化学式: C₇H₁₀O₄
• mdl: MFCD01725790
• 分子量: 158.154
• InChiKey: YUFJCZZAZUVXGI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.1
• 重原子数：
  11
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.714
• 拓扑面积：
  63.6
• 氢给体数：
  1
• 氢受体数：
  4

安全信息

• 海关编码：
  2932209090

反应信息

• 作为反应物：
  描述：

  2-Oxo-3-<2-carboxy-ethyl>-tetrahydrofuran 在 碘 、 2-肟氰乙酸乙酯 、 N,N'-二异丙基碳二亚胺 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成 N,N'-(disulfanediylbis(ethane-2,1-diyl))bis(3-(2-oxotetrahydrofuran-3-yl)propanamide)
  参考文献：
  名称：

  Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules

  摘要：

  Protein-protein interactions (PPIs) are involved in many of life's essential biological functions yet are also an underlying cause of several human diseases, including amyloidosis. The modulation of PPIs presents opportunities to gain mechanistic insights into amyloid assembly, particularly through the use of methods which can trap specific intermediates for detailed study. Such information can also provide a starting point for drug discovery. Here, we demonstrate that covalently tethered small molecule fragments can be used to stabilize specific oligomers during amyloid fibril formation, facilitating the structural characterization of these assembly intermediates. We exemplify the power of covalent tethering using the naturally occurring truncated variant (ΔN6) of the human protein β2-microglobulin (β2m), which assembles into amyloid fibrils associated with dialysis-related amyloidosis. Using this approach, we have trapped tetramers formed by ΔN6 under conditions which would normally lead to fibril formation and found that the degree of tetramer stabilization depends on the site of the covalent tether and the nature of the protein-fragment interaction. The covalent protein-ligand linkage enabled structural characterization of these trapped, off-pathway oligomers using X-ray crystallography and NMR, providing insight into why tetramer stabilization inhibits amyloid assembly. Our findings highlight the power of "post-translational chemical modification" as a tool to study biological molecular mechanisms.

  DOI：

  10.1021/jacs.0c10629
• 作为产物：
  描述：

  alkaline earth salt of/the/ methylsulfuric acid 生成 2-Oxo-3-<2-carboxy-ethyl>-tetrahydrofuran
  参考文献：
  名称：

  McRae et al., Canadian Journal of Research, Section B: Chemical Sciences, 1943, vol. 21, p. 186,191

  摘要：

  DOI：

文献信息

• Conjugate addition of imidazolines: a protocol for 1,4-addition to enones and other acceptors
  作者：Raymond C.F. Jones、Simon C. Hirst

  DOI：10.1016/s0040-4039(01)93787-6

  日期：1989.1
• McRae et al., Canadian Journal of Research, Section B: Chemical Sciences, 1943, vol. 21, p. 186,191
  作者：McRae et al.

  DOI：——

  日期：——
• JPH03251579A
  申请人：——

  公开号：JPH03251579A

  公开（公告）日：1991-11-11
• METABOLISM PROBES FOR THERAPY AND DIAGNOSIS
  申请人：Vanderbilt University

  公开号：US20170283387A1

  公开（公告）日：2017-10-05

  Novel 2-substituted glutamylanides useful as modulators of ASCT2 inhibitors. Compounds of the present invention can be used to treat patients suffering from diseases caused or influenced by abnormal ASCT2 transporter dysfunction.
• Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules
  作者：Emma E. Cawood、Nicolas Guthertz、Jessica S. Ebo、Theodoros K. Karamanos、Sheena E. Radford、Andrew J. Wilson

  DOI：10.1021/jacs.0c10629

  日期：2020.12.9

  Protein-protein interactions (PPIs) are involved in many of life's essential biological functions yet are also an underlying cause of several human diseases, including amyloidosis. The modulation of PPIs presents opportunities to gain mechanistic insights into amyloid assembly, particularly through the use of methods which can trap specific intermediates for detailed study. Such information can also provide a starting point for drug discovery. Here, we demonstrate that covalently tethered small molecule fragments can be used to stabilize specific oligomers during amyloid fibril formation, facilitating the structural characterization of these assembly intermediates. We exemplify the power of covalent tethering using the naturally occurring truncated variant (ΔN6) of the human protein β2-microglobulin (β2m), which assembles into amyloid fibrils associated with dialysis-related amyloidosis. Using this approach, we have trapped tetramers formed by ΔN6 under conditions which would normally lead to fibril formation and found that the degree of tetramer stabilization depends on the site of the covalent tether and the nature of the protein-fragment interaction. The covalent protein-ligand linkage enabled structural characterization of these trapped, off-pathway oligomers using X-ray crystallography and NMR, providing insight into why tetramer stabilization inhibits amyloid assembly. Our findings highlight the power of "post-translational chemical modification" as a tool to study biological molecular mechanisms.