N-benzoyl-O-serine benzylamide | 147019-85-0

• 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: N-benzoyl-O-serine benzylamide
• 英文别名: N-[(2S)-1-(benzylamino)-3-[bis[(4-chlorophenyl)methoxy]phosphinothioyloxy]-1-oxopropan-2-yl]benzamide
• CAS: 147019-85-0
• 化学式: C₃₁H₂₉Cl₂N₂O₅PS
• 分子量: 643.527
• InChiKey: HHIPGQXIPAASJD-LJAQVGFWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.3
• 重原子数：
  42
• 可旋转键数：
  14
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.16
• 拓扑面积：
  118
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-benzoyl-O-serine benzylamide 在 三甲基溴硅烷 、 苯硫酚 、 间甲酚 、 三氟乙酸 作用下， 反应 1.0h， 以88%的产率得到N-benzoyl-O-phosphorothioylserine benzylamide ammonium salt
  参考文献：
  名称：

  Solid-phase synthesis of O-phosphorothioylserine- and -threonine-containing peptides as well as of O-phosphoserine- and -threonine-containing peptides

  摘要：

  This paper describes the synthesis of O-phosphorothioylserine, -threonine, and -tyrosine by sulfurization of the intermediate phosphite triester using phenylacetyl disulfide. Several deprotection procedures were investigated to find the optimal conditions necessary for obtaining the deprotected phosphorothioate amino acids. This method could then be extended to the preparation of O-phosphorothioylserine-and-threonine-containing pentapeptides on a solid phase. After completion of the synthesis of the peptides on the solid support, the amino acid residue containing the free hydroxyl function was phosphitylated using NN-diisopropylbis(4-chlorobenzyl)phosphoramidite and subsequently sulfurized using phenylacetyl disulfide. Silylitic cleavage of the protecting groups, using thiophenol and m-cresol as scavengers, gave the pure deprotected phosphorothioylated peptides. The corresponding phosphopeptides were obtained when the phosphitylated peptides attached to the solid support were oxidized instead of sulfurized using tert-butyl hydroperoxide. To demonstrate that these methods were equally suitable for the synthesis of larger phosphopeptides or phosphorothioate peptides, we prepared the phospho- and the phosphorothioate analog of a pentadecapeptide (H-Leu-Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu-OH) comprising the regulatory phosphorylation site, i.e., serine-14 of phosphorylase b. This example also illustrates that phosphorylation as well as phosphorothioylation is possible of a specified serine residue.

  DOI：

  10.1021/jo00058a006
• 作为产物：
  描述：

  二(4-氯苄基)二异丙基氨基磷酸酯 、 N-benzoylserine benzylamide 在 四氮唑 、 二硫化二苯乙酰 作用下， 生成 N-benzoyl-O-serine benzylamide
  参考文献：
  名称：

  Solid-phase synthesis of O-phosphorothioylserine- and -threonine-containing peptides as well as of O-phosphoserine- and -threonine-containing peptides

  摘要：

  This paper describes the synthesis of O-phosphorothioylserine, -threonine, and -tyrosine by sulfurization of the intermediate phosphite triester using phenylacetyl disulfide. Several deprotection procedures were investigated to find the optimal conditions necessary for obtaining the deprotected phosphorothioate amino acids. This method could then be extended to the preparation of O-phosphorothioylserine-and-threonine-containing pentapeptides on a solid phase. After completion of the synthesis of the peptides on the solid support, the amino acid residue containing the free hydroxyl function was phosphitylated using NN-diisopropylbis(4-chlorobenzyl)phosphoramidite and subsequently sulfurized using phenylacetyl disulfide. Silylitic cleavage of the protecting groups, using thiophenol and m-cresol as scavengers, gave the pure deprotected phosphorothioylated peptides. The corresponding phosphopeptides were obtained when the phosphitylated peptides attached to the solid support were oxidized instead of sulfurized using tert-butyl hydroperoxide. To demonstrate that these methods were equally suitable for the synthesis of larger phosphopeptides or phosphorothioate peptides, we prepared the phospho- and the phosphorothioate analog of a pentadecapeptide (H-Leu-Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu-OH) comprising the regulatory phosphorylation site, i.e., serine-14 of phosphorylase b. This example also illustrates that phosphorylation as well as phosphorothioylation is possible of a specified serine residue.

  DOI：

  10.1021/jo00058a006

文献信息

• Solid-phase synthesis of O-phosphorothioylserine- and -threonine-containing peptides as well as of O-phosphoserine- and -threonine-containing peptides
  作者：Dries B. A. De Bont、Wilna J. Moree、Jacques H. Van Boom、Rob M. J. Liskamp

  DOI：10.1021/jo00058a006

  日期：1993.3

  This paper describes the synthesis of O-phosphorothioylserine, -threonine, and -tyrosine by sulfurization of the intermediate phosphite triester using phenylacetyl disulfide. Several deprotection procedures were investigated to find the optimal conditions necessary for obtaining the deprotected phosphorothioate amino acids. This method could then be extended to the preparation of O-phosphorothioylserine-and-threonine-containing pentapeptides on a solid phase. After completion of the synthesis of the peptides on the solid support, the amino acid residue containing the free hydroxyl function was phosphitylated using NN-diisopropylbis(4-chlorobenzyl)phosphoramidite and subsequently sulfurized using phenylacetyl disulfide. Silylitic cleavage of the protecting groups, using thiophenol and m-cresol as scavengers, gave the pure deprotected phosphorothioylated peptides. The corresponding phosphopeptides were obtained when the phosphitylated peptides attached to the solid support were oxidized instead of sulfurized using tert-butyl hydroperoxide. To demonstrate that these methods were equally suitable for the synthesis of larger phosphopeptides or phosphorothioate peptides, we prepared the phospho- and the phosphorothioate analog of a pentadecapeptide (H-Leu-Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu-OH) comprising the regulatory phosphorylation site, i.e., serine-14 of phosphorylase b. This example also illustrates that phosphorylation as well as phosphorothioylation is possible of a specified serine residue.