N-(2-sulfanylethyl)-2-(4-hydroxyphenyl)acetamide | 1332494-24-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: N-(2-sulfanylethyl)-2-(4-hydroxyphenyl)acetamide
• 英文别名: 2-(4-hydroxyphenyl)-N-(2-sulfanylethyl)acetamide
• CAS: 1332494-24-2
• 化学式: C₁₀H₁₃NO₂S
• mdl: MFCD24389160
• 分子量: 211.285
• InChiKey: ZOYJLDQAKNYMTB-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  50.3
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-(2-sulfanylethyl)-2-(4-hydroxyphenyl)acetamide 在 碘 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 2.0h， 生成 N,N'-(disulfanediylbis(ethane-2,1-diyl))bis(2-(4-hydroxyphenyl)acetamide)
  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：

  对羟基苯乙酸 、 巯基乙胺 在 2-乙氧基-1-乙氧碳酰基-1,2-二氢喹啉 作用下， 以 四氢呋喃 为溶剂， 以70%的产率得到N-(2-sulfanylethyl)-2-(4-hydroxyphenyl)acetamide
  参考文献：
  名称：

  聚恶唑啉热响应性胶束作为放射性核素传递系统。

  摘要：

  热响应性聚合物胶束是有前途的药物和放射性核素载体，对实体瘤具有很强的被动靶向作用。我们已合成ABA三嵌段共聚物的聚[2-甲基-2- oxazoline-块- （2-异丙基-2- oxazoline- ç邻- 2-丁基-2-恶唑啉） -嵌段-2-甲基-2-恶唑啉]。这些聚合物在热响应中心嵌段的浊点温度（CPT）以下且在CPT上方以CMC 5–10×10 -5  g•mL -1的直径≈200nm形成聚合物胶束时，以分子溶解在水溶液中。在模型条件下，引入共聚物中的酚基部分使放射性核素的碘125标记收率很高，并具有足够的体外稳定性。

  DOI：

  10.1002/mabi.201000034