(2R,3R,5S,8R,10S)-benzyl 2-((1R,3R)-1-(tert-butyldimethylsilyloxy)-3-methyl-6-(trimethylsilyl)hex-5-ynyl)-8,10-dimethyl-3-(triethylsilyloxy)-1-oxa-6-azaspiro[4.5]decane-6-carboxylate | 918310-80-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 氮杂螺癸烷衍生物
• 英文名称: (2R,3R,5S,8R,10S)-benzyl 2-((1R,3R)-1-(tert-butyldimethylsilyloxy)-3-methyl-6-(trimethylsilyl)hex-5-ynyl)-8,10-dimethyl-3-(triethylsilyloxy)-1-oxa-6-azaspiro[4.5]decane-6-carboxylate
• CAS: 918310-80-2
• 化学式: C₄₀H₇₁NO₅Si₃
• 分子量: 730.264
• InChiKey: ZXUWQJHOOIQQEU-JIWMHIJYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  10.86
• 重原子数：
  49.0
• 可旋转键数：
  13.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  57.23
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (2R,3R,5S,8R,10S)-benzyl 2-((1R,3R)-1-(tert-butyldimethylsilyloxy)-3-methyl-6-(trimethylsilyl)hex-5-ynyl)-8,10-dimethyl-3-(triethylsilyloxy)-1-oxa-6-azaspiro[4.5]decane-6-carboxylate 在 N-碘代丁二酰亚胺 、 silver trifluoroacetate 作用下， 以 丙酮 为溶剂， 反应 0.17h， 以95%的产率得到(2R,3R,5S,8R,10S)-benzyl 2-((1R,3R)-1-(tert-butyldimethylsilyloxy)-6-iodo-3-methylhex-5-ynyl)-8,10-dimethyl-3-(triethylsilyloxy)-1-oxa-6-azaspiro[4.5]decane-6-carboxylate
  参考文献：
  名称：

  Antibodies with Broad Specificity to Azaspiracids by Use of Synthetic Haptens

  摘要：

  The development of general, sensitive, portable, and quantitative assays for the azaspiracid (AZA) class of marine toxins is urgently needed. Use of a synthetic hapten containing rings F-I of AZA to generate antibodies that cross-react with the AZAs via their common C28-C40 domain and use of these antibodies in ELISA and immunoaffinity columns are reported. This approach has many advantages over using intact azaspiracids (AZAs) derived from environmental samples or total synthesis as haptens for antibody development. A derivative of the levorotatory C28-C40 azaspiracid domain (1) was synthesized efficiently using a one-pot Staudinger reduction/intramolecular aza-Wittig reaction-imine capture sequence to form the H-I ring spiroaminal and a double intramolecluar hetero-Michael addition to assemble the F-G ring ketal. Conjugation of the hapten 1 to cBSA and immunization in sheep generated antibodies that recognized and bound to ovalbumin-conjugated 1 in the absence of AZA1. This binding was inhibited by 1 in a concentration-dependent manner. A mixture of AZA1, AZA2, AZA3, and AZA6 caused a degree of inhibition of antibody binding consistent with its total AZA content, rather than just its content of AZA1. This result suggests that the antibodies also have a similar affinity for AZA2, AZA3, and AZA6 as they do for AZA1 and that such antibodies are suitable for analysis of AZAs in shellfish samples.

  DOI：

  10.1021/ja066971h
• 作为产物：
  描述：

  (2R,3R,8R,10S)-2-((1R,3R)-1-(tert-butyldimethylsilyloxy)-3-methyl-6-(trimethylsilyl)hex-5-ynyl)-8,10-dimethyl-3-(triethylsilyloxy)-1-oxa-6-azaspiro[4.5]decane 、 氯甲酸苄酯 在 potassium carbonate 作用下， 以 二氯甲烷 为溶剂， 反应 12.0h， 以122.6 mg的产率得到(2R,3R,5S,8R,10S)-benzyl 2-((1R,3R)-1-(tert-butyldimethylsilyloxy)-3-methyl-6-(trimethylsilyl)hex-5-ynyl)-8,10-dimethyl-3-(triethylsilyloxy)-1-oxa-6-azaspiro[4.5]decane-6-carboxylate
  参考文献：
  名称：

  Antibodies with Broad Specificity to Azaspiracids by Use of Synthetic Haptens

  摘要：

  The development of general, sensitive, portable, and quantitative assays for the azaspiracid (AZA) class of marine toxins is urgently needed. Use of a synthetic hapten containing rings F-I of AZA to generate antibodies that cross-react with the AZAs via their common C28-C40 domain and use of these antibodies in ELISA and immunoaffinity columns are reported. This approach has many advantages over using intact azaspiracids (AZAs) derived from environmental samples or total synthesis as haptens for antibody development. A derivative of the levorotatory C28-C40 azaspiracid domain (1) was synthesized efficiently using a one-pot Staudinger reduction/intramolecular aza-Wittig reaction-imine capture sequence to form the H-I ring spiroaminal and a double intramolecluar hetero-Michael addition to assemble the F-G ring ketal. Conjugation of the hapten 1 to cBSA and immunization in sheep generated antibodies that recognized and bound to ovalbumin-conjugated 1 in the absence of AZA1. This binding was inhibited by 1 in a concentration-dependent manner. A mixture of AZA1, AZA2, AZA3, and AZA6 caused a degree of inhibition of antibody binding consistent with its total AZA content, rather than just its content of AZA1. This result suggests that the antibodies also have a similar affinity for AZA2, AZA3, and AZA6 as they do for AZA1 and that such antibodies are suitable for analysis of AZAs in shellfish samples.

  DOI：

  10.1021/ja066971h