3,5-di-O-benzoyl-D-ribofuranosyl chloride | 63592-86-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3,5-di-O-benzoyl-D-ribofuranosyl chloride
• 英文别名: 3,5-di-O-benzoylribosyl chloride；3,5-dibenzoylribosyl chloride；D-Ribofuranosyl chloride, 3,5-dibenzoate；[(2R,3S,4R)-3-benzoyloxy-5-chloro-4-hydroxyoxolan-2-yl]methyl benzoate
• CAS: 63592-86-9
• 化学式: C₁₉H₁₇ClO₆
• 分子量: 376.793
• InChiKey: GPDGGKCIUOCYFB-HJNZIYBASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  26
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.26
• 拓扑面积：
  82.1
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  3,5-di-O-benzoyl-D-ribofuranosyl chloride 在 三乙胺 作用下， 以 甲醇 、 二氯甲烷 、 水 为溶剂， 生成 clitidine
  参考文献：
  名称：

  克利替丁，一种来自克霉菌的新有毒吡啶核苷

  摘要：

  从有毒蘑菇Clitocybe acromelalga中分离出一种新的核苷可力丁（1）作为有毒成分。根据光谱数据和化学降解研究推导该结构为1。通过4-氨基烟酸甲酯与3，5-二-O-苯甲酰基-D-呋喃呋喃糖基氯的缩合反应合成1，证实了其结构，包括绝对构型。

  DOI：

  10.1016/0040-4020(82)80107-5
• 作为产物：
  描述：

  1,3,5-三苯甲酰基-D-呋喃核糖 在 盐酸 作用下， 以 四氯化碳 为溶剂， 生成 3,5-di-O-benzoyl-D-ribofuranosyl chloride
  参考文献：
  名称：

  Selective inhibition of Trypanosoma cruzi GAPDH by “bi-substrate” analogues

  摘要：

  一种新的“双底物”类药物系列已被合成，作为甘油醛-3-磷酸脱氢酶的潜在抑制剂，并且已鉴定出一种主要化合物，该化合物对克氏锥虫的该酶具有良好的亲和力和非常高（50倍）的特异性。

  DOI：

  10.1039/b504703j

文献信息

• Simple Synthesis of the 5-O-Benzoylriboside of 1,4-Dihydronicotinic Acid; a Cofactor for DT Diaphorase and Nitroreductase Enzymes
  作者：Lawrence Davies

  DOI：10.1080/15257779508012369

  日期：1995.5.1

  A simple one flask synthesis of the 5-O-benzoylriboside and riboside of nicotinic acid has been developed. Reduction of the benzoylriboside with sodium dithionite gives the 1,4-dihydronicotinic acid in good yield.
• Virtual cofactors for an Escherichia coli nitroreductase enzyme: Relevance to reductively activated prodrugs in antibody directed enzyme prodrug therapy (ADEPT)
  作者：Richard J. Knox、Frank Friedlos、Michael Jarman、Lawrence C. Davies、Phyllis Goddard、Gillian M. Anlezark、Roger G. Melton、Roger F. Sherwood

  DOI：10.1016/0006-2952(95)00077-d

  日期：1995.5

  A nitroreductase enzyme has been isolated from Escherichia coli that has the unusual property of being equally capable of using either NADH or NADPH as a cofactor for the reduction of its substrates which include menadione as well as 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954). This property is shared with the mammalian enzyme, DT diaphorase. The nitroreductase can, like DT diaphorase, also use simple reduced pyridinium compounds as virtual cofactors. The intact NAD(P)H molecule is not required and the simplest quaternary (and therefore reducible) derivative of nicotinamide, 1-methylnicotinamide (reduced), is as effective as NAD(P)H in its ability to act as an electron donor for the nitroreductase. The structure-activity relationship is not identical to that of DT diaphorase and nicotinic acid riboside (reduced) is selective, being active only for the nitroreductase. Irrespective of the virtual cofactor used, the nitroreductase formed the same reduction products of CB 1954 (the 2- and 4-hydroxylamino derivatives in equal proportions). Nicotinic acid riboside (reduced), unlike NADH, was stable to metabolism by serum enzymes and had a plasma half-life of seven minutes in the mouse after an i.v. bolus administration. NADH had an unmeasurably short half-life. Nicotinic acid riboside (reduced) could also be produced in vivo by administration of nicotinic acid 5'-O-benzoyl riboside (reduced). These results demonstrate that the requirement for a cofactor need not be a limitation in the use of reductive enzymes in antibody directed enzyme prodrug therapy (ADEPT). It is proposed that the E. coli nitroreductase would be a suitable enzyme for ADEPT in combination with CB 1954 and a synthetic, enzyme-selective, virtual cofactor such as nicotinic acid riboside (reduced).