[4-I-Phe⁴]Leu-ENK | 295358-45-1

• 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: [4-I-Phe⁴]Leu-ENK
• 英文别名: H-Tyr-Gly-Gly-(4-I)Phe-Leu-OH；H-Tyr-Gly-Gly-4-iodo-Phe-Leu-OH；H-Tyr-Gly-Gly-Phe(4-I)-Leu-OH；(2S)-2-[[(2S)-2-[[2-[[2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]acetyl]amino]-3-(4-iodophenyl)propanoyl]amino]-4-methylpentanoic acid
• CAS: 295358-45-1
• 化学式: C₂₈H₃₆IN₅O₇
• 分子量: 681.528
• InChiKey: TZKSQXWJNRYXTO-VABKMULXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.7
• 重原子数：
  41
• 可旋转键数：
  15
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  200
• 氢给体数：
  7
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  [4-I-Phe⁴]Leu-ENK 、 (4-甲氧基苯基)三氟硼酸钾 在 potassium phosphate 、 trisodium tris(3-sulfophenyl)phosphine 、 palladium diacetate 作用下， 以 水 为溶剂， 反应 24.0h， 生成 H-Tyr-Gly-Gly-Phe-[p-(4-OMe-Ph)]-Leu-OH
  参考文献：
  名称：

  Arylation of Phe and Tyr Side Chains of Unprotected Peptides by a Suzuki−Miyaura Reaction in Water

  摘要：

  An efficient arylation in water of tyrosine and phenylalanine side chains from unprotected iodopeptides is accomplished by using Suzuki-Miyaura cross-coupling processes. The method is compatible with the hydrophilic and thermolabile nature of biologically active peptides. Also of interest, the arylated tyrosine peptides can be accessed in one-pot mode starting from native peptides.

  DOI：

  10.1021/ol801009z
• 作为产物：
  描述：

  Fmoc-甘氨酸 、 Fmoc-L-亮氨酸 、 Fmoc-O-叔丁基-L-酪氨酸 、 Fmoc-L-4-碘苯丙氨酸 在 1-羟基苯并三唑 、 N,N'-二异丙基碳二亚胺 、 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以36 mg的产率得到[4-I-Phe⁴]Leu-ENK
  参考文献：
  名称：

  Modulation of the Interaction between a Peptide Ligand and a G Protein-Coupled Receptor by Halogen Atoms

  摘要：

  Systematic halogenation of two native opioid peptides has shown that halogen atoms can modulate peptide receptor interactions in different manners. First, halogens may produce a steric hindrance that reduces the binding of the peptide to the receptor. Second, chlorine, bromine, or iodine may improve peptide binding if their positive sigma-hole forms a halogen bond interaction with negatively charged atoms of the protein. Lastly, the negative electrostatic potential of fluorine can interact with positively charged atoms of the protein to improve peptide binding.

  DOI：

  10.1021/acsmedchemlett.5b00126

文献信息

• Modulation of the Interaction between a Peptide Ligand and a G Protein-Coupled Receptor by Halogen Atoms
  作者：Mònica Rosa、Gianluigi Caltabiano、Katy Barreto-Valer、Verónica Gonzalez-Nunez、José C. Gómez-Tamayo、Ana Ardá、Jesús Jiménez-Barbero、Leonardo Pardo、Raquel E. Rodríguez、Gemma Arsequell、Gregorio Valencia

  DOI：10.1021/acsmedchemlett.5b00126

  日期：2015.8.13

  Systematic halogenation of two native opioid peptides has shown that halogen atoms can modulate peptide receptor interactions in different manners. First, halogens may produce a steric hindrance that reduces the binding of the peptide to the receptor. Second, chlorine, bromine, or iodine may improve peptide binding if their positive sigma-hole forms a halogen bond interaction with negatively charged atoms of the protein. Lastly, the negative electrostatic potential of fluorine can interact with positively charged atoms of the protein to improve peptide binding.
• Arylation of Phe and Tyr Side Chains of Unprotected Peptides by a Suzuki−Miyaura Reaction in Water
  作者：Maria Vilaró、Gemma Arsequell、Gregorio Valencia、Alfredo Ballesteros、José Barluenga

  DOI：10.1021/ol801009z

  日期：2008.8.7

  An efficient arylation in water of tyrosine and phenylalanine side chains from unprotected iodopeptides is accomplished by using Suzuki-Miyaura cross-coupling processes. The method is compatible with the hydrophilic and thermolabile nature of biologically active peptides. Also of interest, the arylated tyrosine peptides can be accessed in one-pot mode starting from native peptides.