4-cyano-N-(2-mercaptoethyl)benzamide

• 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: 4-cyano-N-(2-mercaptoethyl)benzamide
• 英文别名: 4-cyano-N-(2-sulfanylethyl)benzamide
• 化学式: C₁₀H₁₀N₂OS
• mdl: MFCD24388791
• 分子量: 206.268
• InChiKey: BJWNGOCUTQHHFE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  14
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  53.9
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  4-cyano-N-(2-mercaptoethyl)benzamide 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(4-cyanobenzamide)
  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：

  对氰基苯甲酰氯 、 巯基乙胺 在 吡啶 、 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 18.0h， 以19.3%的产率得到4-cyano-N-(2-mercaptoethyl)benzamide
  参考文献：
  名称：

  Internal Standard in Surface-Enhanced Raman Spectroscopy

  摘要：

  本文介绍了一种在表面增强拉曼光谱中使用 SAM 层作为校准内部标准的方法。通过金属硫键将三种含氰化合物附着到金胶体上，并对其光谱稳定性和归一化能力进行了评估。结果表明，分析物罗丹明 6G 和内标信号增强是共变的，可以用 PLS 对分析物进行定量。增强基质是信号增强变化较大的混沌集合体，这表明该方法具有多功能性。

  DOI：

  10.1021/ac0491298

文献信息

• 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.
• Internal Standard in Surface-Enhanced Raman Spectroscopy
  作者：A. Lorén、J. Engelbrektsson、C. Eliasson、M. Josefson、J. Abrahamsson、M. Johansson、K. Abrahamsson

  DOI：10.1021/ac0491298

  日期：2004.12.1

  A method is presented for the use of SAM layers as internal standards for calibration in surface-enhanced Raman spectroscopy. Three cyano-containing compounds were attached to gold colloids via a metal−sulfur bond and evaluated for spectral stability and normalization capacity. The results show that the analyte, rhodamine 6G, and the internal standard signal enhancement covaried, and it was possible to quantify the analyte with PLS. The fact that the enhancing substrate was chaotic assemblies with large variation in signal enhancement shows the versatility of this method.

  本文介绍了一种在表面增强拉曼光谱中使用 SAM 层作为校准内部标准的方法。通过金属硫键将三种含氰化合物附着到金胶体上，并对其光谱稳定性和归一化能力进行了评估。结果表明，分析物罗丹明 6G 和内标信号增强是共变的，可以用 PLS 对分析物进行定量。增强基质是信号增强变化较大的混沌集合体，这表明该方法具有多功能性。