α-N-Fmoc-L-thioaspartate-2-amino-5-nitroanilide | 1520083-31-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: α-N-Fmoc-L-thioaspartate-2-amino-5-nitroanilide
• 英文别名: tert-butyl (3S)-4-(2-amino-5-nitroanilino)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-sulfanylidenebutanoate
• CAS: 1520083-31-1
• 化学式: C₂₉H₃₀N₄O₆S
• 分子量: 562.646
• InChiKey: UVEOKABSIJNCEE-VWLOTQADSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.6
• 重原子数：
  40
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.28
• 拓扑面积：
  181
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  α-N-Fmoc-L-thioaspartate-2-amino-5-nitroanilide 在 溶剂黄146 、 sodium nitrite 作用下， 以 水 为溶剂， 反应 0.5h， 生成 tert-butyl (3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-4-(6-nitrobenzotriazol-1-yl)-4-sulfanylidenebutanoate
  参考文献：
  名称：

  Efficient Site-Specific Incorporation of Thioamides into Peptides on a Solid Support

  摘要：

  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.

  DOI：

  10.1021/acs.orglett.5b01484
• 作为产物：
  描述：

  4-硝基邻苯二胺 在 劳森试剂 、 6-chloro-3-((dimethylamino)(dimethyliminio)methyl)-1H-benzo[d][1,2,3]triazol-3-ium-1-olatehexafluorophosphate(V) 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 24.0h， 生成 α-N-Fmoc-L-thioaspartate-2-amino-5-nitroanilide
  参考文献：
  名称：

  Efficient Site-Specific Incorporation of Thioamides into Peptides on a Solid Support

  摘要：

  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.

  DOI：

  10.1021/acs.orglett.5b01484

文献信息

• Efficient, Traceless Semi-Synthesis of α-Synuclein Labeled with a Fluoro­phore/Thioamide FRET Pair
  作者：E. Petersson、Rebecca Wissner、Anne Wagner、John Warner

  DOI：10.1055/s-0033-1339853

  日期：——

  incorporated into proteins through semi-synthesis and used as probes to monitor structural changes. To date, our methods have required the presence of a cysteine at the peptide ligation site, which may not be present in the native peptide sequence. Here, we present a strategy for the semi-synthesis of thioproteins using homocysteine as a ligation point with subsequent masking as methionine, making the ligation

  我们已经证明硫代酰胺可以通过半合成掺入蛋白质中，并用作探针来监测结构变化。迄今为止，我们的方法需要在肽连接位点存在半胱氨酸，这可能不存在于天然肽序列中。在这里，我们提出了一种半合成硫蛋白的策略，使用同型半胱氨酸作为连接点，随后掩蔽为甲硫氨酸，使连接“无痕”。
• 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.