2-[2-[2-[bis[2-(6-aminohexanoylamino)ethyl]carbamoyloxy]ethoxy]ethoxy]ethyl N,N-bis[2-(6-aminohexanoylamino)ethyl]carbamate | 169744-22-3

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 2-[2-[2-[bis[2-(6-aminohexanoylamino)ethyl]carbamoyloxy]ethoxy]ethoxy]ethyl N,N-bis[2-(6-aminohexanoylamino)ethyl]carbamate
• CAS: 169744-22-3
• 化学式: C₄₀H₈₀N₁₀O₁₀
• 分子量: 861.136
• InChiKey: OMVMNXHNPUBHNX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.8
• 重原子数：
  60
• 可旋转键数：
  43
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.85
• 拓扑面积：
  298
• 氢给体数：
  8
• 氢受体数：
  14

反应信息

• 作为反应物：
  描述：

  4-硝基苯酚溴乙酯 、 2-[2-[2-[bis[2-(6-aminohexanoylamino)ethyl]carbamoyloxy]ethoxy]ethoxy]ethyl N,N-bis[2-(6-aminohexanoylamino)ethyl]carbamate 在 碳酸氢钠 作用下， 以 1,4-二氧六环 为溶剂， 反应 1.0h， 以46%的产率得到1,2-ethanediylbis(oxy-2,1-ethanediylbis<2-<<6-<(bromoacetyl)amino>-1-oxohexyl>amino>ethyl>carbamate)
  参考文献：
  名称：

  Immunospecific Reduction of Antioligonucleotide Antibody-Forming Cells with a Tetrakis-oligonucleotide Conjugate (LJP 394), a Therapeutic Candidate for the Treatment of Lupus Nephritis

  摘要：

  A discrete tetravalent conjugate, 7a (LJP 394), consisting of four oligonucleotides attached to a common carrier or platform was prepared. Single-stranded oligonucleotide 20-mers consisting of alternating deoxycytidine-deoxyadenosine nucleotides, (CA)(10), were attached to a tetrabro-moacetylated platform by displacement with sulfhydryl-terminated linkers. The tetrabro-moacetylated platform 3a was synthesized in three steps using triethylene glycol bis-(chloroformate). The single-stranded conjugate was characterized by polyacrylamide gel electrophoresis, DNA sequencing, phosphate analysis, carbon and nitrogen combustion analysis, and correlation of stoichiometry to conversion in the conjugation process. HPLC and capillary electrophoretic methods were developed to evaluate purity. The tetrakis, single-stranded conjugate was annealed with a stoichiometric amount of a complementary single-stranded oligonucleotide 20-mer consisting of alternating thymidine-deoxyguanosine nucleotides, (TG)(10). The double-stranded conjugate LJP 394 was characterized by melt temperature and hyperchromicity, phosphate analysis, and carbon and nitrogen combustion analysis. LJP 394 inhibits binding of DNA to anti-double-stranded oligonucleotide antibodies and reduces anti-oligonucleotide-specific plaque (antibody)-forming cells in an immunized mouse model by a proposed mechanism involving cross-linking B cell surface immunoglobins.

  DOI：

  10.1021/jm00012a013
• 作为产物：
  描述：

  三甘醇双氯甲酸酯 在 palladium on activated charcoal 吡啶 、 环己烯 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 生成 2-[2-[2-[bis[2-(6-aminohexanoylamino)ethyl]carbamoyloxy]ethoxy]ethoxy]ethyl N,N-bis[2-(6-aminohexanoylamino)ethyl]carbamate
  参考文献：
  名称：

  Immunospecific Reduction of Antioligonucleotide Antibody-Forming Cells with a Tetrakis-oligonucleotide Conjugate (LJP 394), a Therapeutic Candidate for the Treatment of Lupus Nephritis

  摘要：

  A discrete tetravalent conjugate, 7a (LJP 394), consisting of four oligonucleotides attached to a common carrier or platform was prepared. Single-stranded oligonucleotide 20-mers consisting of alternating deoxycytidine-deoxyadenosine nucleotides, (CA)(10), were attached to a tetrabro-moacetylated platform by displacement with sulfhydryl-terminated linkers. The tetrabro-moacetylated platform 3a was synthesized in three steps using triethylene glycol bis-(chloroformate). The single-stranded conjugate was characterized by polyacrylamide gel electrophoresis, DNA sequencing, phosphate analysis, carbon and nitrogen combustion analysis, and correlation of stoichiometry to conversion in the conjugation process. HPLC and capillary electrophoretic methods were developed to evaluate purity. The tetrakis, single-stranded conjugate was annealed with a stoichiometric amount of a complementary single-stranded oligonucleotide 20-mer consisting of alternating thymidine-deoxyguanosine nucleotides, (TG)(10). The double-stranded conjugate LJP 394 was characterized by melt temperature and hyperchromicity, phosphate analysis, and carbon and nitrogen combustion analysis. LJP 394 inhibits binding of DNA to anti-double-stranded oligonucleotide antibodies and reduces anti-oligonucleotide-specific plaque (antibody)-forming cells in an immunized mouse model by a proposed mechanism involving cross-linking B cell surface immunoglobins.

  DOI：

  10.1021/jm00012a013

文献信息

• Immunospecific Reduction of Antioligonucleotide Antibody-Forming Cells with a Tetrakis-oligonucleotide Conjugate (LJP 394), a Therapeutic Candidate for the Treatment of Lupus Nephritis
  作者：David S. Jones、Paul A. Barstad、Mark J. Feild、John P. Hachmann、Merle S. Hayag、Kenneth W. Hill、G. Michael Iverson、Douglas A. Livingston、Moorthy S. Palanki

  DOI：10.1021/jm00012a013

  日期：1995.6

  A discrete tetravalent conjugate, 7a (LJP 394), consisting of four oligonucleotides attached to a common carrier or platform was prepared. Single-stranded oligonucleotide 20-mers consisting of alternating deoxycytidine-deoxyadenosine nucleotides, (CA)(10), were attached to a tetrabro-moacetylated platform by displacement with sulfhydryl-terminated linkers. The tetrabro-moacetylated platform 3a was synthesized in three steps using triethylene glycol bis-(chloroformate). The single-stranded conjugate was characterized by polyacrylamide gel electrophoresis, DNA sequencing, phosphate analysis, carbon and nitrogen combustion analysis, and correlation of stoichiometry to conversion in the conjugation process. HPLC and capillary electrophoretic methods were developed to evaluate purity. The tetrakis, single-stranded conjugate was annealed with a stoichiometric amount of a complementary single-stranded oligonucleotide 20-mer consisting of alternating thymidine-deoxyguanosine nucleotides, (TG)(10). The double-stranded conjugate LJP 394 was characterized by melt temperature and hyperchromicity, phosphate analysis, and carbon and nitrogen combustion analysis. LJP 394 inhibits binding of DNA to anti-double-stranded oligonucleotide antibodies and reduces anti-oligonucleotide-specific plaque (antibody)-forming cells in an immunized mouse model by a proposed mechanism involving cross-linking B cell surface immunoglobins.