| 1539312-16-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• CAS: 1539312-16-7
• 化学式: C₂₆H₂₃N₅O₄S
• 分子量: 501.566
• InChiKey: BTBUPKITHRGNPC-DEOSSOPVSA-N

物化性质

• 密度：
  1.43±0.1 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.08
• 重原子数：
  36.0
• 可旋转键数：
  6.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.23
• 拓扑面积：
  112.18
• 氢给体数：
  1.0
• 氢受体数：
  8.0

反应信息

• 作为产物：
  描述：

  (9H-fluoren-9-yl)methyl (S)-(1-((2-amino-5-nitrophenyl)amino)-3-methyl-1-thioxobutan-2-yl)carbamate 在 溶剂黄146 、 sodium nitrite 作用下， 生成
  参考文献：
  名称：

  N-糖基化肽的位点特异性制备：天冬氨酸的硫代酰胺定向激活

  摘要：

  在肽中引入主链硫代酰胺键的单原子 (O→S) 取代促进了 Ag I促进的 Asn N-糖肽的位点特异性生成。

  DOI：

  10.1002/anie.202210367

文献信息

• Synthesis of thioester peptides for the incorporation of thioamides into proteins by native chemical ligation
  作者：Solongo Batjargal、Yun Huang、Yanxin J. Wang、E. James Petersson

  DOI：10.1002/psc.2589

  日期：2014.2

  Thioamides can be used as photoswitches, as reporters of local environment, as inhibitors of enzymes, and as fluorescence quenchers. We have recently demonstrated the incorporation of thioamides into polypeptides and proteins using native chemical ligation (NCL). In this protocol, we describe procedures for the synthesis of a thioamide precursor and an NCL‐ready thioamide‐containing peptide using Dawson's

  硫代酰胺可用作光开关、局部环境报告器、酶抑制剂和荧光猝灭剂。我们最近证明了使用天然化学连接 (NCL) 将硫代酰胺掺入多肽和蛋白质中。在该协议中，我们描述了使用 Dawson 的N-酰基-苯并咪唑啉酮 (Nbz) 工艺合成硫代酰胺前体和 NCL-ready 含硫代酰胺肽的程序。我们包括对神经元蛋白α-突触核蛋白的硫代酰胺标记片段的 NCL 合成的描述。版权所有 © 2014 欧洲肽学会和 John Wiley & Sons, Ltd.
• Efficient Site-Specific Incorporation of Thioamides into Peptides on a Solid Support
  作者：Somnath Mukherjee、Hitesh Verma、Jayanta Chatterjee

  DOI：10.1021/acs.orglett.5b01484

  日期：2015.6.19

  Designing bioactive peptides containing thioamide functionality to modulate their pharmacological properties has been thwarted so far because of various synthetic challenges. The fast, efficient, and inexpensive synthesis and incorporation of a wide range of thionated amino acids into a growing peptide chain on a solid support is reported using standard Fmoc-based chemistry. The commonly employed methodology is comprehensively investigated and optimized with significant improvements regarding the quantity of reagents and reaction conditions. The utility of the protocol is further demonstrated in the synthesis of dithionated linear and monothionated cyclic peptides, which has been a daunting task.