Boc-Asn-Phe-OBn | 42002-17-5

• 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: Boc-Asn-Phe-OBn
• 英文别名: L-Phenylalanine, N2-[(1,1-dimethylethoxy)carbonyl]-L-asparaginyl-, phenylmethyl ester；benzyl (2S)-2-[[(2S)-4-amino-2-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutanoyl]amino]-3-phenylpropanoate
• CAS: 42002-17-5
• 化学式: C₂₅H₃₁N₃O₆
• 分子量: 469.538
• InChiKey: WKFSSMDSJPZGIK-PMACEKPBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  34
• 可旋转键数：
  13
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  137
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Boc-Asn-Phe-OBn 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 0.5h， 以94%的产率得到Asn-Phe-OBn trifluoroacetate
  参考文献：
  名称：

  Dimerization Inhibitors of HIV-1 Protease Based on a Bicyclic Guanidinium Subunit

  摘要：

  Original inhibitors of HIV-1 protease based on a chiral bicyclic guanidinium scaffold linked to short peptidic mimics of the terminal protease sequences and to a lipophilic group were designed. These inhibitors prevent dimerization of the native protease by an interfacial structure at the highly conserved antiparallel beta-strand involving both the N and C termini that substantially account for dimerization. The preorganized guanidinium spacer introduces additional electrostatic hydrogen-bonding interactions with the C-terminal Phe-99 carboxylate. Lipophilic residues linked to side chains and the guanidinium scaffold are essential for dimerization inhibition as ascertained by Zhang kinetics (4, K-id = 290 nM; 6 or 6', K-id = 150 nM; 8, K-id = 400 nM) combined with a circular dichroism study on the enzyme thermal stability. Remarkably, less hydrophobic compounds result in mixed dimerization (1a and 3) or active site inhibitors (5). Removal of the guanidinium hydrophobic groups leads to less active or inactive ligands.

  DOI：

  10.1021/jm030871u
• 作为产物：
  描述：

  BOC-L-天冬酰胺 、 L-苯丙氨酸苄酯对甲苯磺酸盐 在 1-羟基苯并三唑 、 N,N-二异丙基乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 为溶剂， 反应 5.0h， 以96%的产率得到Boc-Asn-Phe-OBn
  参考文献：
  名称：

  Dimerization Inhibitors of HIV-1 Protease Based on a Bicyclic Guanidinium Subunit

  摘要：

  Original inhibitors of HIV-1 protease based on a chiral bicyclic guanidinium scaffold linked to short peptidic mimics of the terminal protease sequences and to a lipophilic group were designed. These inhibitors prevent dimerization of the native protease by an interfacial structure at the highly conserved antiparallel beta-strand involving both the N and C termini that substantially account for dimerization. The preorganized guanidinium spacer introduces additional electrostatic hydrogen-bonding interactions with the C-terminal Phe-99 carboxylate. Lipophilic residues linked to side chains and the guanidinium scaffold are essential for dimerization inhibition as ascertained by Zhang kinetics (4, K-id = 290 nM; 6 or 6', K-id = 150 nM; 8, K-id = 400 nM) combined with a circular dichroism study on the enzyme thermal stability. Remarkably, less hydrophobic compounds result in mixed dimerization (1a and 3) or active site inhibitors (5). Removal of the guanidinium hydrophobic groups leads to less active or inactive ligands.

  DOI：

  10.1021/jm030871u

文献信息

• Dimerization Inhibitors of HIV-1 Protease Based on a Bicyclic Guanidinium Subunit
  作者：Perla Breccia、Nicole Boggetto、Ruth Pérez-Fernández、Michiel Van Gool、Masayuki Takahashi、Loïc René、Pilar Prados、Bernard Badet、Michèle Reboud-Ravaux、Javier de Mendoza

  DOI：10.1021/jm030871u

  日期：2003.11.1

  Original inhibitors of HIV-1 protease based on a chiral bicyclic guanidinium scaffold linked to short peptidic mimics of the terminal protease sequences and to a lipophilic group were designed. These inhibitors prevent dimerization of the native protease by an interfacial structure at the highly conserved antiparallel beta-strand involving both the N and C termini that substantially account for dimerization. The preorganized guanidinium spacer introduces additional electrostatic hydrogen-bonding interactions with the C-terminal Phe-99 carboxylate. Lipophilic residues linked to side chains and the guanidinium scaffold are essential for dimerization inhibition as ascertained by Zhang kinetics (4, K-id = 290 nM; 6 or 6', K-id = 150 nM; 8, K-id = 400 nM) combined with a circular dichroism study on the enzyme thermal stability. Remarkably, less hydrophobic compounds result in mixed dimerization (1a and 3) or active site inhibitors (5). Removal of the guanidinium hydrophobic groups leads to less active or inactive ligands.