L-亮氨酰-L-亮氨酰-L-酪氨酸 | 20368-24-5

• 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
• 中文名称: L-亮氨酰-L-亮氨酰-L-酪氨酸
• 英文名称: Leu-Leu-Tyr
• 英文别名: (2S)-2-[[(2S)-2-[[(2S)-2-azaniumyl-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]-3-(4-hydroxyphenyl)propanoate
• CAS: 20368-24-5
• 化学式: C₂₁H₃₃N₃O₅
• mdl: MFCD00057825
• 分子量: 407.51
• InChiKey: UCNNZELZXFXXJQ-BZSNNMDCSA-N

物化性质

• 沸点：
  695.2±55.0 °C(Predicted)
• 密度：
  1.173
• 溶解度：
  DMSO（少许）、水（少许）

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  29
• 可旋转键数：
  11
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.571
• 拓扑面积：
  142
• 氢给体数：
  5
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  L-亮氨酰-L-亮氨酰-L-酪氨酸 生成
  参考文献：
  名称：

  IVR 是否发生在肽离子解离之前？

  摘要：

  通过时间分辨光解 (TRPD) 研究小肽离子。中性肽的激光解吸与离子阱中的激光光电离结合，然后进行热化、激光光解和飞行时间质量分析。离子化和激发通过肽 C 端的芳香发色团发生，而解离在 N 端产生亚铵离子。目的是揭示分子内振动再分布 (IVR) 在肽自由基阳离子的单分子断裂中的作用，其激发是位点选择性的。虽然以前的实验集中在质谱上，但这里采用的途径是确定微规范速率常数。对于具有相同发色团、经历相同碎裂但具有不同数量的自由度的两种肽，在相当明确的内能 E 下测量速率常数。∼102−105 s-1 范围内的实验速率测量将...

  DOI：

  10.1021/jp030275b
• 作为产物：
  描述：

  BOC-亮氨酰-亮氨酸 在 三乙基硅烷 、 碳酸氢钠 、 三氟乙酸 作用下， 以 1,4-二氧六环 、 水 、 乙酸乙酯 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成 L-亮氨酰-L-亮氨酰-L-酪氨酸
  参考文献：
  名称：

  Antibody Recognition of Chiral Surfaces. Enantiomorphous Crystals of Leucine-Leucine-Tyrosine

  摘要：

  Monoclonal antibodies were selected after immunization with crystals of the tripeptide L-leucine-L-leucine-L-tyrosine. They interact with the tripeptide crystals, but do not interact with the tripeptide molecule, with other crystalline surfaces, or with adsorbed protein. The interactions of two antibodies with crystals of L-Leu-L-Leu-L-Tyr and of its enantiomer D-LeU-D-Leu-D-Tyr were characterized in depth. Antibody 48E is stereoselective and enantioselective: it recognizes only the {0(1) over bar 1} faces of the L-Leu-L-Leu-L-Tyr crystals, and not the enantiomorphous {01(1) over bar} faces of D-Leu-D-Leu-D-Tyr crystals, or any other faces of either crystal. In contrast antibody 602E is poorly stereoselectiwe and is not enantioselective: it recognizes the crystals of both enantiomers, interacting With a number of different faces of each. The different recognition patterns are explained on the basis of the nature of the interactions and the structure of the interacting surfaces. Understanding this antibody specificity advances our general understanding of surface recognition and transfer of chiral information across biological interfaces.

  DOI：

  10.1021/ja027942j

文献信息

• Antibody Recognition of Chiral Surfaces. Enantiomorphous Crystals of Leucine-Leucine-Tyrosine
  作者：Merav Geva、Felix Frolow、Miriam Eisenstein、Lia Addadi

  DOI：10.1021/ja027942j

  日期：2003.1.1

  Monoclonal antibodies were selected after immunization with crystals of the tripeptide L-leucine-L-leucine-L-tyrosine. They interact with the tripeptide crystals, but do not interact with the tripeptide molecule, with other crystalline surfaces, or with adsorbed protein. The interactions of two antibodies with crystals of L-Leu-L-Leu-L-Tyr and of its enantiomer D-LeU-D-Leu-D-Tyr were characterized in depth. Antibody 48E is stereoselective and enantioselective: it recognizes only the 0(1) over bar 1} faces of the L-Leu-L-Leu-L-Tyr crystals, and not the enantiomorphous 01(1) over bar} faces of D-Leu-D-Leu-D-Tyr crystals, or any other faces of either crystal. In contrast antibody 602E is poorly stereoselectiwe and is not enantioselective: it recognizes the crystals of both enantiomers, interacting With a number of different faces of each. The different recognition patterns are explained on the basis of the nature of the interactions and the structure of the interacting surfaces. Understanding this antibody specificity advances our general understanding of surface recognition and transfer of chiral information across biological interfaces.
• Does IVR Take Place Prior to Peptide Ion Dissociation?
  作者：Yongjun Hu、Boaz Hadas、Mandy Davidovitz、Bülent Balta、Chava Lifshitz

  DOI：10.1021/jp030275b

  日期：2003.8.1

  peptide ions are studied by time-resolved photodissociation (TRPD). Laser desorption of neutral peptides is combined with laser photoionization in an ion trap followed by thermalization, laser photodissociation, and time-of-flight mass analysis. Ionization and excitation take place through an aromatic chromophore at the C-terminus of the peptide, whereas dissociation produces the immonium ion at the

  通过时间分辨光解 (TRPD) 研究小肽离子。中性肽的激光解吸与离子阱中的激光光电离结合，然后进行热化、激光光解和飞行时间质量分析。离子化和激发通过肽 C 端的芳香发色团发生，而解离在 N 端产生亚铵离子。目的是揭示分子内振动再分布 (IVR) 在肽自由基阳离子的单分子断裂中的作用，其激发是位点选择性的。虽然以前的实验集中在质谱上，但这里采用的途径是确定微规范速率常数。对于具有相同发色团、经历相同碎裂但具有不同数量的自由度的两种肽，在相当明确的内能 E 下测量速率常数。∼102−105 s-1 范围内的实验速率测量将...