CILKEPVHGV-NH₂ | 859849-32-4

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: CILKEPVHGV-NH₂
• 英文别名: H-Cys-Ile-Leu-Lys-Glu-Pro-Val-His-Gly-Val-NH2；(4S)-4-[[(2S)-6-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2R)-2-amino-3-sulfanylpropanoyl]amino]-3-methylpentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]amino]-5-[(2S)-2-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-amino-3-methyl-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-5-oxopentanoic acid
• CAS: 859849-32-4
• 化学式: C₄₉H₈₄N₁₄O₁₂S
• 分子量: 1093.36
• InChiKey: FQPUYPJCCAGZTR-ZCYJDOAPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.5
• 重原子数：
  76
• 可旋转键数：
  34
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  415
• 氢给体数：
  14
• 氢受体数：
  16

反应信息

• 作为反应物：
  描述：

  CILKEPVHGV-NH₂ 、 在 3,3,3-膦三基三丙酸 、 4-巯基苯基乙酸 作用下， 以84%的产率得到
  参考文献：
  名称：

  Access to Cyclic or Branched Peptides Using Bis(2-sulfanylethyl)amido Side-Chain Derivatives of Asp and Glu

  摘要：

  Bis(2-sulfanylethyl)amido (SEA) side-chain derivatives of aspartic and glutamic acids enable the synthesis of tail-to-side chain cyclic or branched peptides using standard Fmoc-SPPS followed by SEA native peptide ligation.

  DOI：

  10.1021/ol300528r
• 作为产物：
  描述：

  Fmoc-L-缬氨酸 、 Fmoc-L-亮氨酸 、 Fmoc-L-脯氨酸 、 Fmoc-O-叔丁基-L-谷氨酸 、 Fmoc-Gly-NH2 、 Fmoc-L-异亮氨酸 、 N-alpha-芴甲氧羰基-N-epsilon-叔丁氧羰基-L-赖氨酸 、 (R)-3-tert-Butylsulfanyl-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid 、 N-Fmoc-N'-三苯甲基-L-组氨酸 在 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以55%的产率得到CILKEPVHGV-NH₂
  参考文献：
  名称：

  Bis(2-sulfanylethyl)amido Peptides Enable Native Chemical Ligation at Proline and Minimize Deletion Side-Product Formation

  摘要：

  Native chemical ligation of C-terminal peptidyl prolyl alkylthioesters with N-terminal cysteinyl peptides usually exhibits poor kinetic rates compared to other C-terminal amino acid residues. It is shown here that the reaction is accompanied by the formation of a deletion side product which is minimized by using a bis(2-sulfanylethyl)amido (SEA) thioester surrogate at a mildly acidic pH.

  DOI：

  10.1021/ol402678a

文献信息

• Selectively Activatable Latent Thiol and Selenolesters Simplify the Access to Cyclic or Branched Peptide Scaffolds
  作者：Laurent Raibaut、Hervé Drobecq、Oleg Melnyk

  DOI：10.1021/acs.orglett.5b01817

  日期：2015.7.17

  The cyclic dichalcogenides based on the bis(2-chalcogenoethyl)amide structure are latent N,S (SEA, chalcogen = S) or N,Se (SeEA, chalcogen = Se) acyl Shift systems. The large difference in the reducing potential between SEA and SeEA dichalcogenides allows their sequential and selective activation by reduction. Based on these concepts, one-pot three or four peptide segment assembly processes were designed, facilitating access to branched or cyclic peptide scaffolds.
• Access to Cyclic or Branched Peptides Using Bis(2-sulfanylethyl)amido Side-Chain Derivatives of Asp and Glu
  作者：Emmanuelle Boll、Julien Dheur、Hervé Drobecq、Oleg Melnyk

  DOI：10.1021/ol300528r

  日期：2012.5.4

  Bis(2-sulfanylethyl)amido (SEA) side-chain derivatives of aspartic and glutamic acids enable the synthesis of tail-to-side chain cyclic or branched peptides using standard Fmoc-SPPS followed by SEA native peptide ligation.
• Bis(2-sulfanylethyl)amido Peptides Enable Native Chemical Ligation at Proline and Minimize Deletion Side-Product Formation
  作者：Laurent Raibaut、Phillip Seeberger、Oleg Melnyk

  DOI：10.1021/ol402678a

  日期：2013.11

  Native chemical ligation of C-terminal peptidyl prolyl alkylthioesters with N-terminal cysteinyl peptides usually exhibits poor kinetic rates compared to other C-terminal amino acid residues. It is shown here that the reaction is accompanied by the formation of a deletion side product which is minimized by using a bis(2-sulfanylethyl)amido (SEA) thioester surrogate at a mildly acidic pH.