N~6~-(2,4-Dinitrophenyl)-N~2~-{[(9H-fluoren-9-yl)methoxy]carbonyl}-D-lysine | 269061-41-8

• 物质功能分类: 有机原料 - 羧酸类化合物及衍生物
• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: N~6~-(2,4-Dinitrophenyl)-N~2~-{[(9H-fluoren-9-yl)methoxy]carbonyl}-D-lysine
• 英文别名: (2R)-6-(2,4-dinitroanilino)-2-(9H-fluoren-9-ylmethoxycarbonylamino)hexanoic acid
• CAS: 269061-41-8
• 化学式: C₂₇H₂₆N₄O₈
• 分子量: 534.525
• InChiKey: OENCMORJQAUAAJ-XMMPIXPASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.6
• 重原子数：
  39
• 可旋转键数：
  11
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.26
• 拓扑面积：
  179
• 氢给体数：
  3
• 氢受体数：
  9

反应信息

• 作为反应物：
  描述：

  N~6~-(2,4-Dinitrophenyl)-N~2~-{[(9H-fluoren-9-yl)methoxy]carbonyl}-D-lysine 在 哌啶 、 三氟乙酸 作用下， 以 N,N-二甲基甲酰胺 、 水 、 乙腈 为溶剂， 反应 0.17h， 生成 N^ξ-(2,4-dinitrophenyl)-D-lysine
  参考文献：
  名称：

  Fluorescent Mu Selective Opioid Ligands from a Mixture Based Cyclic Peptide Library

  摘要：

  A positional scanning cyclic peptide library was generated using a penta-peptide thioester scaffold. Glycine was fixed at position R-1. Diaminopropionic acid was fixed at position R-3, with its gamma-amino attaching to an anthraniloyl group. Positions R-2 and R-4 contained 36 L- and D- amino acids and position R-5 contained 19 L- amino acids. Cyclization was performed in a mixture of acetonitrile and 1.5 M aqueous imidazole solution (7:1 v/v) at room temperature for 5 days. No significant cross-oligomerization was detected under the cyclization conditions. The library was screened in a binding assay for mu opioid receptor, identifying the active amino acid mixture at each position. A total of 40 individual cyclic peptides were identified and synthesized by the combinations of the most active amino acid mixtures found at three positions 5 x 4 x 2. Two cyclic peptides exhibited high binding affinities to opioid receptor. The most active cyclic peptide in the library was yielded to have Tyr at R-2, D-Lys at R-4, and Tyr at R-5. Further investigation on this compound revealed the side chain-to-tail isomer to have greater binding affinity (14 nM) than the head-to-tail isomer (39 nM). Both isomers were selective for the mu-opioid receptor.

  DOI：

  10.1021/co300110t
• 作为产物：
  描述：

  N-alpha-芴甲氧羰基-N-epsilon-叔丁氧羰基-D-赖氨酸 在 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 0.67h， 生成 N~6~-(2,4-Dinitrophenyl)-N~2~-{[(9H-fluoren-9-yl)methoxy]carbonyl}-D-lysine
  参考文献：
  名称：

  Fluorescent Mu Selective Opioid Ligands from a Mixture Based Cyclic Peptide Library

  摘要：

  A positional scanning cyclic peptide library was generated using a penta-peptide thioester scaffold. Glycine was fixed at position R-1. Diaminopropionic acid was fixed at position R-3, with its gamma-amino attaching to an anthraniloyl group. Positions R-2 and R-4 contained 36 L- and D- amino acids and position R-5 contained 19 L- amino acids. Cyclization was performed in a mixture of acetonitrile and 1.5 M aqueous imidazole solution (7:1 v/v) at room temperature for 5 days. No significant cross-oligomerization was detected under the cyclization conditions. The library was screened in a binding assay for mu opioid receptor, identifying the active amino acid mixture at each position. A total of 40 individual cyclic peptides were identified and synthesized by the combinations of the most active amino acid mixtures found at three positions 5 x 4 x 2. Two cyclic peptides exhibited high binding affinities to opioid receptor. The most active cyclic peptide in the library was yielded to have Tyr at R-2, D-Lys at R-4, and Tyr at R-5. Further investigation on this compound revealed the side chain-to-tail isomer to have greater binding affinity (14 nM) than the head-to-tail isomer (39 nM). Both isomers were selective for the mu-opioid receptor.

  DOI：

  10.1021/co300110t

文献信息

• Fluorescent Mu Selective Opioid Ligands from a Mixture Based Cyclic Peptide Library
  作者：Yangmei Li、Colette T. Dooley、Jaime A. Misler、Ginamarie Debevec、Marc A. Giulianotti、Margaret E. Cazares、Laura Maida、Richard A. Houghten

  DOI：10.1021/co300110t

  日期：2012.12.10

  A positional scanning cyclic peptide library was generated using a penta-peptide thioester scaffold. Glycine was fixed at position R-1. Diaminopropionic acid was fixed at position R-3, with its gamma-amino attaching to an anthraniloyl group. Positions R-2 and R-4 contained 36 L- and D- amino acids and position R-5 contained 19 L- amino acids. Cyclization was performed in a mixture of acetonitrile and 1.5 M aqueous imidazole solution (7:1 v/v) at room temperature for 5 days. No significant cross-oligomerization was detected under the cyclization conditions. The library was screened in a binding assay for mu opioid receptor, identifying the active amino acid mixture at each position. A total of 40 individual cyclic peptides were identified and synthesized by the combinations of the most active amino acid mixtures found at three positions 5 x 4 x 2. Two cyclic peptides exhibited high binding affinities to opioid receptor. The most active cyclic peptide in the library was yielded to have Tyr at R-2, D-Lys at R-4, and Tyr at R-5. Further investigation on this compound revealed the side chain-to-tail isomer to have greater binding affinity (14 nM) than the head-to-tail isomer (39 nM). Both isomers were selective for the mu-opioid receptor.