N-Phthaloyl-L-Phe-Val-OH | 98131-22-7

• 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-Phthaloyl-L-Phe-Val-OH
• 英文别名: Pht
• CAS: 98131-22-7
• 化学式: C₂₂H₂₂N₂O₅
• 分子量: 394.427
• InChiKey: OLSSIALGSLLVNT-ROUUACIJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  29
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  104
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-Phthaloyl-L-Phe-Val-OH 在 氯化亚砜 、 乙二胺 作用下， 以 乙醇 、 二氯甲烷 、 水 为溶剂， 反应 16.0h， 生成 H-Phe-Val-OMe
  参考文献：
  名称：

  Site-Selective C(sp³)–H Functionalization of Di-, Tri-, and Tetrapeptides at the N-Terminus

  摘要：

  Although the syntheses of novel and diverse peptides rely mainly on traditional coupling using unnatural amino acids, postsynthetic modification of peptides could provide a complementary method for the preparation of nonproteinogenic peptides. Site selectivity of postsynthetic modification of peptides is usually achieved by targeting reactive moieties, such as the thiol group of cysteine or the C-2 position of tryptophan. Herein, we report the development of site-selective functionalizations of inert C(sp(3))-H bonds of N-terminal amino acids in di-, tri-, and tetrapeptides without installing a directing group. The native amino acid moiety within the peptide is used as a ligand to accelerate the C-H activation reaction. In the long run, this newly uncovered reactivity could provide guidance for developing site-selective C(sp(3))-H activation toward postsynthetic modification of a broader range of peptides.

  DOI：

  10.1021/ja510233h
• 作为产物：
  描述：

  邻苯二甲酰基-L-丙氨酸 在 N-甲基吗啉 、 N-羟基-7-氮杂苯并三氮唑 、 palladium 10% on activated carbon 、 氢气 、 silver(I) acetate 、 palladium diacetate 、 lithium fluoride 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 甲醇 、 乙酸乙酯 、 N,N-二甲基甲酰胺 为溶剂， 反应 27.5h， 生成 N-Phthaloyl-L-Phe-Val-OH
  参考文献：
  名称：

  Site-Selective C(sp³)–H Functionalization of Di-, Tri-, and Tetrapeptides at the N-Terminus

  摘要：

  Although the syntheses of novel and diverse peptides rely mainly on traditional coupling using unnatural amino acids, postsynthetic modification of peptides could provide a complementary method for the preparation of nonproteinogenic peptides. Site selectivity of postsynthetic modification of peptides is usually achieved by targeting reactive moieties, such as the thiol group of cysteine or the C-2 position of tryptophan. Herein, we report the development of site-selective functionalizations of inert C(sp(3))-H bonds of N-terminal amino acids in di-, tri-, and tetrapeptides without installing a directing group. The native amino acid moiety within the peptide is used as a ligand to accelerate the C-H activation reaction. In the long run, this newly uncovered reactivity could provide guidance for developing site-selective C(sp(3))-H activation toward postsynthetic modification of a broader range of peptides.

  DOI：

  10.1021/ja510233h

文献信息

• Efficient microwave-assisted synthesis of 4-amino-2-benzazepin-3-ones as conformationally restricted dipeptide mimetics
  作者：Beatrice Severino、Ferdinando Fiorino、Antonella Esposito、Francesco Frecentese、Francesca De Angelis、Elisa Perissutti、Giuseppe Caliendo、Vincenzo Santagada

  DOI：10.1016/j.tet.2008.10.072

  日期：2009.1

  In this paper, we describe the synthesis of conformationally constrained dipeptide mimetic derivatives. Microwave flash heating was used in several synthetic steps providing the opportunity to perform the reactions in dramatically shortened time as well as to increase the obtained yields. The efficiency of the methodology makes it useful in order to prepare other dipeptides containing the 4-amino-

  在本文中，我们描述了构象受限的二肽模拟衍生物的合成。微波闪蒸加热用于几个合成步骤中，从而提供了在大大缩短的时间内进行反应以及提高产率的机会。该方法的效率使其可用于制备含有4-氨基-四氢-2-苯并ze杂-3-酮基序的其他二肽。
• Site-Selective C(sp³)–H Functionalization of Di-, Tri-, and Tetrapeptides at the N-Terminus
  作者：Wei Gong、Guofu Zhang、Tao Liu、Ramesh Giri、Jin-Quan Yu

  DOI：10.1021/ja510233h

  日期：2014.12.3

  Although the syntheses of novel and diverse peptides rely mainly on traditional coupling using unnatural amino acids, postsynthetic modification of peptides could provide a complementary method for the preparation of nonproteinogenic peptides. Site selectivity of postsynthetic modification of peptides is usually achieved by targeting reactive moieties, such as the thiol group of cysteine or the C-2 position of tryptophan. Herein, we report the development of site-selective functionalizations of inert C(sp(3))-H bonds of N-terminal amino acids in di-, tri-, and tetrapeptides without installing a directing group. The native amino acid moiety within the peptide is used as a ligand to accelerate the C-H activation reaction. In the long run, this newly uncovered reactivity could provide guidance for developing site-selective C(sp(3))-H activation toward postsynthetic modification of a broader range of peptides.