N-(4-pentenoyl)-4[(4’;1’,1”)biphenyl]-L-phenylalanine pdCpA ester | 1451156-28-7

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - （3'->5'）-二核苷酸和类似物
• 英文名称: N-(4-pentenoyl)-4[(4’;1’,1”)biphenyl]-L-phenylalanine pdCpA ester
• CAS: 1451156-28-7
• 化学式: C₄₅H₄₉N₉O₁₅P₂
• 分子量: 1017.88
• InChiKey: ULKFCLNGUVUJPK-VZTRNXQZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.34
• 重原子数：
  71.0
• 可旋转键数：
  20.0
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  347.14
• 氢给体数：
  7.0
• 氢受体数：
  21.0

反应信息

• 作为产物：
  描述：

  Boc-4-碘-L-苯丙氨酸 在 四(三苯基膦)钯 、 lithium hydroxide monohydrate 、 碳酸氢钠 、 sodium carbonate 、 三乙胺 、 三氟乙酸 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 、 甲苯 、 乙腈 为溶剂， 反应 152.0h， 生成 N-(4-pentenoyl)-4[(4’;1’,1”)biphenyl]-L-phenylalanine pdCpA ester
  参考文献：
  名称：

  Detection of Dihydrofolate Reductase Conformational Change by FRET Using Two Fluorescent Amino Acids

  摘要：

  Two fluorescent amino acids, including the novel fluorescent species 4-biphenyl-L-phenylalanine (1), have been incorporated at positions 17 and 115 of dihydrofolate reductase (DHFR) to enable a study of conformational changes associated with inhibitor binding. Unlike most studies involving fluorescently labeled proteins, the fluorophores were incorporated into the amino acid side chains, and both probes [1 and L-(7-hydroxycoumarin-4-yl)ethylglycine (2)] were smaller than fluorophores typically used for such studies. The DHFR positions were chosen as potentially useful for Forster resonance energy transfer (FRET) measurements on the basis of their estimated separation (17-18 angstrom) and the expected change in distance along the reaction coordinate. Also of interest was the steric accessibility of the two sites: Glu17 is on the surface of DHFR, while Ile115 is within a folded region of the protein. Modified DHFR I (1 at. position 17; 2 at position 115) and DHFR II (2 at position 17; 1 at position 115) were both catalytically competent. However, DHFR II containing the potentially rotatable biphenylphenylalanine moiety at sterically encumbered position 115 was significantly more active than DHFR I. Irradiation of the modified DHFRs at 280 nm effected excitation of 1, energy transfer to 2, and emission by 2 at 450 nm. However, the energy transfer was substantially more efficient in DHFR II. The effect of inhibitor binding was also measured. Trimethoprim mediated concentration-dependent diminution of the emission observed at 450 nm for DHFR II but not for DHFR I. These findings demonstrate that amino acids containing small fluorophores can be introduced into DHFR with minimal disruption of function and in a fashion that enables sensitive monitoring of changes in DHFR conformation.

  DOI：

  10.1021/ja403007r