2-bromo-5,6-dichloro-5'-O-L-lysyl-1-β-D-ribofuranosylbenzimidazole

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 苯并咪唑核糖核苷和核糖核苷酸
• 英文名称: 2-bromo-5,6-dichloro-5'-O-L-lysyl-1-β-D-ribofuranosylbenzimidazole
• 英文别名: 5'-O-L-lysyl-BDCRB；[(2R,3S,4R,5R)-5-(2-bromo-5,6-dichlorobenzimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl (2S)-2,6-diaminohexanoate
• 化学式: C₁₈H₂₃BrCl₂N₄O₅
• 分子量: 526.214
• InChiKey: PKSUULGPGVQTSW-JMDOCYRQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  30
• 可旋转键数：
  9
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  146
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  N-alpha-叔丁氧羰基-L-赖氨酸 在 4-二甲氨基吡啶 、 N,N'-二环己基碳二亚胺 、 三氟乙酸 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 28.0h， 生成 2-bromo-5,6-dichloro-5'-O-L-lysyl-1-β-D-ribofuranosylbenzimidazole
  参考文献：
  名称：

  Amino Acid Ester Prodrugs of the Antiviral Agent 2-Bromo-5,6-dichloro-1-(β-d-ribofuranosyl)benzimidazole as Potential Substrates of hPEPT1 Transporter

  摘要：

  Amino acid ester prodrugs of 2-bromo-5,6-dichloro-1-(beta-D-ribofuranosyl)benzimidazole (BDCRB) were synthesized and evaluated for their affinity for hPEPT1, an intestinal oligopeptide transporter. Assays of competitive inhibition of [H-3]glycylsarcosine (Gly-Sar) uptake in HeLa/hPEPT1 cells by the amino acid ester prodrugs of BDCRB suggested their 2- to 4-fold higher affinity for hPEPT1 compared to BDCRB. Further, promoieties with hydrophobic side chains and L-configuration were preferred by the hPEPT1 transporter.

  DOI：

  10.1021/jm049450i

文献信息

• Amino Acid Ester Prodrugs of the Antiviral Agent 2-Bromo-5,6-dichloro-1-(β-<scp>d</scp>-ribofuranosyl)benzimidazole as Potential Substrates of hPEPT1 Transporter
  作者：Xueqin Song、Balvinder S. Vig、Philip L. Lorenzi、John C. Drach、Leroy B. Townsend、Gordon L. Amidon

  DOI：10.1021/jm049450i

  日期：2005.2.1

  Amino acid ester prodrugs of 2-bromo-5,6-dichloro-1-(beta-D-ribofuranosyl)benzimidazole (BDCRB) were synthesized and evaluated for their affinity for hPEPT1, an intestinal oligopeptide transporter. Assays of competitive inhibition of [H-3]glycylsarcosine (Gly-Sar) uptake in HeLa/hPEPT1 cells by the amino acid ester prodrugs of BDCRB suggested their 2- to 4-fold higher affinity for hPEPT1 compared to BDCRB. Further, promoieties with hydrophobic side chains and L-configuration were preferred by the hPEPT1 transporter.