O-benzyl-N-Boc-DL-tyrosine benzyl ester | 1155261-19-0

• 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: O-benzyl-N-Boc-DL-tyrosine benzyl ester
• 英文别名: L-Tyrosine, N-[(1,1-dimethylethoxy)carbonyl]-O-(phenylmethyl)-,phenylmethyl ester；benzyl 2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-(4-phenylmethoxyphenyl)propanoate
• CAS: 1155261-19-0
• 化学式: C₂₈H₃₁NO₅
• 分子量: 461.558
• InChiKey: VQXLZJJBXSYFDE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.8
• 重原子数：
  34
• 可旋转键数：
  12
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  73.9
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  O-benzyl-N-Boc-DL-tyrosine benzyl ester 在 盐酸 作用下， 以 乙酸乙酯 为溶剂， 反应 0.33h， 以99%的产率得到O-benzyl-DL-tyrosine benzyl ester hydrochloride
  参考文献：
  名称：

  Anthranilic acid based CCK1 receptor antagonists: Blocking the receptor with the same ‘words’ of the endogenous ligand

  摘要：

  The anthranilic acid diamides represent the more recent class of nonpeptide CCK1 receptor antagonists. This class is characterized by the presence of anthranilic acid, used as a molecular scaffold, and two pharmacophores selected from the C-terminal tetrapeptide of CCK. The lead compound coded VL-0395, endowed with sub-micromolar affinity towards CCK1 receptors, was characterized by the presence of Phe and 2-indole moiety at the C- and N-termini of anthranilic acid, respectively. Herein we describe the first step of the anthranilic acid C- terminal optimization using, instead of Phe, aminoacids belonging to the primary structure of CCK-8 and other not coded residues. Thus we demonstrate that the CCK1 receptor affinity depends on the nature of the aminoacidic side chain as well as that the free carboxy group of the alpha-aminoacids is crucial for the binding. The R enantiomers of the most active compounds represent the eutomers of this class of antagonists confirming thus the stereo preference of the receptor. Moreover this SAR study demonstrates that the receptor binding pocket, that host the aminoacidic side chain, results much more tolerant respect to that accommodating the indole ring. As a result, an appropriate variation of the aminoacidic side chain could provide a better CCK1 receptor affinity diorthosis. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.02.012
• 作为产物：
  描述：

  N-(叔丁氧羰基)-DL-酪氨酸 、 溴甲苯 在 potassium carbonate 作用下， 以 丙酮 为溶剂， 以66%的产率得到O-benzyl-N-Boc-DL-tyrosine benzyl ester
  参考文献：
  名称：

  Anthranilic acid based CCK1 receptor antagonists: Blocking the receptor with the same ‘words’ of the endogenous ligand

  摘要：

  The anthranilic acid diamides represent the more recent class of nonpeptide CCK1 receptor antagonists. This class is characterized by the presence of anthranilic acid, used as a molecular scaffold, and two pharmacophores selected from the C-terminal tetrapeptide of CCK. The lead compound coded VL-0395, endowed with sub-micromolar affinity towards CCK1 receptors, was characterized by the presence of Phe and 2-indole moiety at the C- and N-termini of anthranilic acid, respectively. Herein we describe the first step of the anthranilic acid C- terminal optimization using, instead of Phe, aminoacids belonging to the primary structure of CCK-8 and other not coded residues. Thus we demonstrate that the CCK1 receptor affinity depends on the nature of the aminoacidic side chain as well as that the free carboxy group of the alpha-aminoacids is crucial for the binding. The R enantiomers of the most active compounds represent the eutomers of this class of antagonists confirming thus the stereo preference of the receptor. Moreover this SAR study demonstrates that the receptor binding pocket, that host the aminoacidic side chain, results much more tolerant respect to that accommodating the indole ring. As a result, an appropriate variation of the aminoacidic side chain could provide a better CCK1 receptor affinity diorthosis. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.02.012

文献信息

• [EN] SYNTHETIC HELIZYME ENZYMES
  申请人：THE UNIVERSITY OF COLORADO FOUNDATION, INC.

  公开号：WO1991010733A1

  公开（公告）日：1991-07-25

  (EN) The design and synthesis of peptide molecules which possess catalytic activity are described. Peptide molecules are constructed to contain a selected active site positioned with respect to a selected substrate binding site to achieve a desired substrate specificity. The invention specifically provides catalysts which contain a number of amphiphilic helical peptides bonded at their carboxyl ends to a multifunctional base and having active site residues functional for catalysis positioned within the helix. These peptide-based catalysts are called helizymes. Helizymes having serine protease activity are provided.(FR) Structure et synthèse de molécules de peptides ayant une activité catalytique. On construit des molécules de peptides qui contiennent un site actif sélectionné positionné par rapport à un site de liaison d'un substrat sélectionné afin d'obtenir une spécificité voulue par rapport au substrat. Plus spécifiquement, des catalyseurs contiennent une pluralité de peptides hélicoïdaux amphiphiliques reliés par leurs extrémités carboxyles à une base multifonctionnelle et ayant des résidus catalyseurs au site actif positionnés à l'intérieur de l'hélice. Ces catalyseurs à base de peptides sont appelés hélizymes. L'invention concerne des hélizymes ayant une activitté de protéase de sérine.
• Anthranilic acid based CCK1 receptor antagonists: Blocking the receptor with the same ‘words’ of the endogenous ligand
  作者：Lucia Lassiani、Michela V. Pavan、Federico Berti、George Kokotos、Theodoros Markidis、Laura Mennuni、Francesco Makovec、Antonio Varnavas

  DOI：10.1016/j.bmc.2009.02.012

  日期：2009.3

  The anthranilic acid diamides represent the more recent class of nonpeptide CCK1 receptor antagonists. This class is characterized by the presence of anthranilic acid, used as a molecular scaffold, and two pharmacophores selected from the C-terminal tetrapeptide of CCK. The lead compound coded VL-0395, endowed with sub-micromolar affinity towards CCK1 receptors, was characterized by the presence of Phe and 2-indole moiety at the C- and N-termini of anthranilic acid, respectively. Herein we describe the first step of the anthranilic acid C- terminal optimization using, instead of Phe, aminoacids belonging to the primary structure of CCK-8 and other not coded residues. Thus we demonstrate that the CCK1 receptor affinity depends on the nature of the aminoacidic side chain as well as that the free carboxy group of the alpha-aminoacids is crucial for the binding. The R enantiomers of the most active compounds represent the eutomers of this class of antagonists confirming thus the stereo preference of the receptor. Moreover this SAR study demonstrates that the receptor binding pocket, that host the aminoacidic side chain, results much more tolerant respect to that accommodating the indole ring. As a result, an appropriate variation of the aminoacidic side chain could provide a better CCK1 receptor affinity diorthosis. (C) 2009 Elsevier Ltd. All rights reserved.