methyl N-(propiolyl)-L-phenylalanine | 18450-49-2

• 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: methyl N-(propiolyl)-L-phenylalanine
• 英文别名: methyl propionyl-L-phenylalaninate；methyl propioloyl-L-phenylalaninate；N-propiolyl-Phe-OMe；N-Propioloyl-L-phenylalanin-methylester；methyl (2S)-3-phenyl-2-(prop-2-ynoylamino)propanoate
• CAS: 18450-49-2
• 化学式: C₁₃H₁₃NO₃
• 分子量: 231.251
• InChiKey: IKXLNXUABASHGI-NSHDSACASA-N

物化性质

• 密度：
  1.165±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  17
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.23
• 拓扑面积：
  55.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  methyl N-(propiolyl)-L-phenylalanine 在 sodium hydroxide 作用下， 以 水 为溶剂， 反应 16.0h， 以87%的产率得到(S)-3-Phenyl-2-propynoylamino-propionic acid
  参考文献：
  名称：

  Properties of analogues of an intermediate in the process of mechanism-based inactivation of carboxypeptidase A

  摘要：

  Carboxypeptidase A (CPA), and other zinc-dependent proteases, facilitate an ct deprotonation of judiciously designed ketones and amides. This adventitious reaction has been used in the development of effective mechanism-based inactivators for this family of enzymes. N-Acryloyl-L-phenylalanine, an intermediate in the process of mechanism-based inactivation of CPA by N-(3-chloropropionyl)-L-phenylalanine, was shown to be an affinity inactivator, but also a very poor substrate for the enzyme. Similarly, O-(acryloyl)-L-3-phenyllactate was shown to be both an affinity inactivator and a poor substrate for CPA. However, consistent with the trend established with other ester and amide substrates for CPA, O-(acryloyl)-L-3-phenyllactate is a better substrate than N-acryloyl-L-phenylalanine. N-(Propiolyl)-L-phenylalanine served only as a poor substrate for the enzyme. To gain insight into enzyme inactivation and the unexpected poor turnover of these molecules, molecular modeling of these compounds with the crystal structure of CPA was carried out. These analyses suggested that the smaller size of these molecules permits a binding mode which is somewhat different in the active site than with typical larger substrates, such that the transition-state species for hydrolysis is not greatly stabilized by the enzyme. The slow turnover of these species, along with their specific binding interactions with the enzyme active site have implications for the inactivation chemistry of CPA and other zinc proteases by this family of mechanism-based inactivators. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0968-0896(96)00142-3
• 作为产物：
  描述：

  L-苯丙氨酸甲酯盐酸盐 、 丙炔酸 在 N,N-二异丙基乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 以80%的产率得到methyl N-(propiolyl)-L-phenylalanine
  参考文献：
  名称：

  氨基酸功能化的α-GalCer类似物的合成和生物学活性。

  摘要：

  不变的自然杀伤性T细胞（iNKT细胞）是操纵免疫系统的有希望的靶标，它们的T细胞受体与CD1d呈递的糖脂抗原结合后，可以迅速释放大量Th1和Th2细胞因子。在本文中，我们希望报道一系列新的α-GalCer类似物，这些类似物是通过在糖脂的C-6'位掺入1-氨基酸甲酯合成的。对这些合成类似物在体外和体内刺激iNKT细胞产生Th1和Th2细胞因子的能力的评估表明，它们是有效的CD1d配体，可以刺激鼠脾细胞释放更高的Th1细胞因子IFN-γ。体外。在体内，Gly-α-GalCer（1）和Lys-α-GalCer（3）表现出比α-GalCer更多的Th1偏向反应，尤其是类似物3在体内与α-GalCer（IFN-γ/ IL-4 = 2.5）相比，对IFN-γ产生的选择性最高（IFN-γ/ IL-4 = 5.32）。这些新颖的α-GalCer类似物可用作有效的X射线晶体探针，以揭示α-GalCer/ C

  DOI：

  10.1016/j.bmc.2019.115141

文献信息

• [EN] PYRAZOLE AND PYRAZOLINE-CONTAINING PEPTIDES, HIGH THROUGHPUT CLICK LIBRARIES, AND METHODS<br/>[FR] PEPTIDES À TENEUR EN PYRAZOLE ET PYRAZOLINE, BIBLIOTHÈQUES DE CHIMIE CLICK À HAUT DÉBIT ET PROCÉDÉS ASSOCIÉS
  申请人：UNM RAINFOREST INNOVATIONS

  公开号：WO2022164900A1

  公开（公告）日：2022-08-04

  Pyrazole-containing peptides and pyrazoline containing peptides. The pyrazole- containing peptides and/or the pyrazoline containing peptides may include one or more cyclic peptides. Methods for making pyrazole-containing peptides and pyrazoline containing peptides. The method includes reacting a diazo functionalized amino acid with an alkyne or an alkene functionalized amino acid. Amino acids may be functionalized on the N-terminus and/or the C- terminus.

  含有吡唑基的肽和含有吡唑啉基的肽。这些含有吡唑基和/或含有吡唑啉基的肽可能包括一个或多个环肽。制备含有吡唑基的肽和含有吡唑啉基的肽的方法。该方法包括将一种二氮化物功能化的氨基酸与一种炔基或烯基功能化的氨基酸反应。氨基酸可以在N-末端和/或C-末端上进行功能化。
• Potential Carcinolytic Agents.^1,2 V. Enamine Mustards
  作者：Zinon B. Papanastassiou、Robert J. Bruni、Edward V. White V

  DOI：10.1021/jm00316a040

  日期：1967.7
• Synthesis and biological activities of amino acids functionalized α-GalCer analogues
  作者：Weiwei Ma、Jingjing Bi、Chuanfang Zhao、Zhiguo Zhang、Tongxin Liu、Guisheng Zhang

  DOI：10.1016/j.bmc.2019.115141

  日期：2020.1

  T cell receptor with glycolipid antigens presented by CD1d. In this paper, we wish to report a novel series of α-GalCer analogues which were synthesized by incorporation of l-amino acid methyl esters in the C-6' position of glycolipid. The evaluation of these synthetic analogues for their capacities to stimulate iNKT-cells into producing Th1 and Th2 cytokines both in vitro and in vivo indicated that

  不变的自然杀伤性T细胞（iNKT细胞）是操纵免疫系统的有希望的靶标，它们的T细胞受体与CD1d呈递的糖脂抗原结合后，可以迅速释放大量Th1和Th2细胞因子。在本文中，我们希望报道一系列新的α-GalCer类似物，这些类似物是通过在糖脂的C-6'位掺入1-氨基酸甲酯合成的。对这些合成类似物在体外和体内刺激iNKT细胞产生Th1和Th2细胞因子的能力的评估表明，它们是有效的CD1d配体，可以刺激鼠脾细胞释放更高的Th1细胞因子IFN-γ。体外。在体内，Gly-α-GalCer（1）和Lys-α-GalCer（3）表现出比α-GalCer更多的Th1偏向反应，尤其是类似物3在体内与α-GalCer（IFN-γ/ IL-4 = 2.5）相比，对IFN-γ产生的选择性最高（IFN-γ/ IL-4 = 5.32）。这些新颖的α-GalCer类似物可用作有效的X射线晶体探针，以揭示α-GalCer/ C
• Properties of analogues of an intermediate in the process of mechanism-based inactivation of carboxypeptidase A
  作者：Soumitra S. Ghosh、Srikanth Dakoji、Yasuhiro Tanaka、Young J. Cho、Shahriar Mobashery

  DOI：10.1016/0968-0896(96)00142-3

  日期：1996.9

  Carboxypeptidase A (CPA), and other zinc-dependent proteases, facilitate an ct deprotonation of judiciously designed ketones and amides. This adventitious reaction has been used in the development of effective mechanism-based inactivators for this family of enzymes. N-Acryloyl-L-phenylalanine, an intermediate in the process of mechanism-based inactivation of CPA by N-(3-chloropropionyl)-L-phenylalanine, was shown to be an affinity inactivator, but also a very poor substrate for the enzyme. Similarly, O-(acryloyl)-L-3-phenyllactate was shown to be both an affinity inactivator and a poor substrate for CPA. However, consistent with the trend established with other ester and amide substrates for CPA, O-(acryloyl)-L-3-phenyllactate is a better substrate than N-acryloyl-L-phenylalanine. N-(Propiolyl)-L-phenylalanine served only as a poor substrate for the enzyme. To gain insight into enzyme inactivation and the unexpected poor turnover of these molecules, molecular modeling of these compounds with the crystal structure of CPA was carried out. These analyses suggested that the smaller size of these molecules permits a binding mode which is somewhat different in the active site than with typical larger substrates, such that the transition-state species for hydrolysis is not greatly stabilized by the enzyme. The slow turnover of these species, along with their specific binding interactions with the enzyme active site have implications for the inactivation chemistry of CPA and other zinc proteases by this family of mechanism-based inactivators. Copyright (C) 1996 Elsevier Science Ltd