N-(9-fluorenylmethoxycarbonyl)-L-phenylalanyl-N-ethyl-S-triphenylmethyl-L-cysteine | 1334511-48-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N-(9-fluorenylmethoxycarbonyl)-L-phenylalanyl-N-ethyl-S-triphenylmethyl-L-cysteine
• 英文别名: Fmoc-Phe-(Et)Cys(Trt)-OH；Fmoc-Phe-N(Et)Cys(Trt)-OH；(2R)-2-[ethyl-[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-phenylpropanoyl]amino]-3-tritylsulfanylpropanoic acid
• CAS: 1334511-48-6
• 化学式: C₄₈H₄₄N₂O₅S
• 分子量: 760.954
• InChiKey: IPLKMOUTRICBME-CXNSMIOJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.9
• 重原子数：
  56
• 可旋转键数：
  16
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  121
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-(9-fluorenylmethoxycarbonyl)-L-phenylalanyl-N-ethyl-S-triphenylmethyl-L-cysteine 、 1-羟基苯并三唑 在 N,N'-二异丙基碳二亚胺 作用下， 以 1,2-二氯乙烷 为溶剂， 反应 0.08h， 生成
  参考文献：
  名称：

  Peptidyl N-alkylcysteine as a peptide thioester surrogate in the native chemical ligation

  摘要：

  Peptides having the C-terminal N-alkylcysteine (NAC) with a free carboxy group, which can be easily prepared by the conventional 9-fluorenylmethoxycarbonyl (Fmoc) solid-phase peptide synthesis (SPPS), was directly used for the native chemical ligation (NCL) based on the in situ thioesterification method. The reaction efficiently proceeded under a mild acidic condition (pH similar to 5) to give the ligated product. This method was successfully used for the synthesis of the human brain natriuretic peptide, (BNP)-32, showing the usefulness of the peptidyl NAC as a thioester surrogate for the NCL reaction. (C) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2015.01.095
• 作为产物：
  描述：

  N-ethyl-S-trityl-L-cysteine 、 N-芴甲氧羰基-L-苯丙氨酸五氟苯酯 在 3-羟基-1,2,3-苯并三嗪-4(3H)-酮 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 以74%的产率得到N-(9-fluorenylmethoxycarbonyl)-L-phenylalanyl-N-ethyl-S-triphenylmethyl-L-cysteine
  参考文献：
  名称：

  Efficient preparation of Fmoc-aminoacyl-N-ethylcysteine unit, a key device for the synthesis of peptide thioesters

  摘要：

  描述了Fmoc-氨酰-N-乙基-S-三苯基甲基半胱氨酸的合成，这是一种用于通过Fmoc-SPPS（固相肽合成）制备肽硫酯的N至S-酰基迁移装置。在DMF中，在HOOBt（3-羟基-3,4-二氢-4-氧代-1,2,3-苯并三氮唑）的存在下，Fmoc-氨酰五氟苯基酯与N-乙基-S-三苯基甲基半胱氨酸的缩合反应有效进行。在反应过程中产生的小量非对映体可以通过HPLC纯化轻松分离，绝大多数蛋白源氨基酸获得了高纯度的迁移装置。

  DOI：

  10.1039/c1ob05831b

文献信息

• Efficient preparation of Fmoc-aminoacyl-N-ethylcysteine unit, a key device for the synthesis of peptide thioesters
  作者：Hironobu Hojo、Hajime Kobayashi、Risa Ubagai、Yuya Asahina、Yuko Nakahara、Hidekazu Katayama、Yukishige Ito、Yoshiaki Nakahara

  DOI：10.1039/c1ob05831b

  日期：——

  The synthesis of Fmoc-aminoacyl-N-ethyl-S-triphenylmethylcysteine, an N- to S-acyl migratory device for the preparation of peptide thioesters by Fmoc-SPPS (solid-phase peptide synthesis) is described. Condensation of Fmoc-aminoacyl pentafluorophenyl ester and N-ethyl-S-triphenylmethylcysteine was efficiently performed in the presence of HOOBt (3-hydroxy-3,4-dihydro-4-oxo-1,2,3-benzotriazine) in DMF. A small amount of diastereomer yielded during the reaction was easily separated by HPLC purification and the highly pure devices were obtained for most of the proteinogenic amino acids.

  描述了Fmoc-氨酰-N-乙基-S-三苯基甲基半胱氨酸的合成，这是一种用于通过Fmoc-SPPS（固相肽合成）制备肽硫酯的N至S-酰基迁移装置。在DMF中，在HOOBt（3-羟基-3,4-二氢-4-氧代-1,2,3-苯并三氮唑）的存在下，Fmoc-氨酰五氟苯基酯与N-乙基-S-三苯基甲基半胱氨酸的缩合反应有效进行。在反应过程中产生的小量非对映体可以通过HPLC纯化轻松分离，绝大多数蛋白源氨基酸获得了高纯度的迁移装置。
• Peptidyl N-alkylcysteine as a peptide thioester surrogate in the native chemical ligation
  作者：Yuya Asahina、Kei Nabeshima、Hironobu Hojo

  DOI：10.1016/j.tetlet.2015.01.095

  日期：2015.3

  Peptides having the C-terminal N-alkylcysteine (NAC) with a free carboxy group, which can be easily prepared by the conventional 9-fluorenylmethoxycarbonyl (Fmoc) solid-phase peptide synthesis (SPPS), was directly used for the native chemical ligation (NCL) based on the in situ thioesterification method. The reaction efficiently proceeded under a mild acidic condition (pH similar to 5) to give the ligated product. This method was successfully used for the synthesis of the human brain natriuretic peptide, (BNP)-32, showing the usefulness of the peptidyl NAC as a thioester surrogate for the NCL reaction. (C) 2015 Elsevier Ltd. All rights reserved.