methyl 1-(pyridin-4-ylmethyl)-3,6-dihydro-2H-pyridine-5-carboxylate | 1452109-12-4

• 分子结构分类: 有机化合物 - 生物碱及其衍生物
• 英文名称: methyl 1-(pyridin-4-ylmethyl)-3,6-dihydro-2H-pyridine-5-carboxylate
• CAS: 1452109-12-4
• 化学式: C₁₃H₁₆N₂O₂
• 分子量: 232.282
• InChiKey: UKCNIZTUADUTOD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  17
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  42.4
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  methyl 1-(pyridin-4-ylmethyl)-3,6-dihydro-2H-pyridine-5-carboxylate 在 水 、 sodium hydroxide 作用下， 以 甲醇 为溶剂， 反应 2.5h， 以85%的产率得到sodium 1-(pyridin-4-ylmethyl)-1,2,5,6-tetrahydropyridine-3-carboxylate
  参考文献：
  名称：

  N-Heteroarylmethyl-5-hydroxy-1,2,5,6-tetrahydropyridine-3-carboxylic acid a novel scaffold for the design of uncompetitive α-glucosidase inhibitors

  摘要：

  The enzyme alpha-glucosidase has attracted interest owing to its involvement in the digestive process of carbohydrate, its role in intracellular glycoprotein trafficking, tumorigenesis and viral infection. In this study, several members of a new family of N-heteroarylmethyl substituted azasugars were synthesized and evaluated as alpha-glucosidase inhibitors. We systematically investigated the effect of different N-substituents as well as the role of hydroxyl and carboxylate moieties on the piperidine ring. The compounds N-heteroarylmethyl-5-hydroxy-1,2,5,6-tetrahydropyridine-3-carboxylic acid emerged as potent alpha-glucosidase inhibitors. Unlike Acarbose and other clinically relevant alpha-glucosidase inhibitors, these compounds act through a reversible uncompetitive mechanism of inhibition which make them attractive candidates for drug development. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.07.012
• 作为产物：
  描述：

  氢溴酸槟榔碱 在 1-氯乙基氯甲酸酯 、 碳酸氢钠 、 sodium carbonate 、 1,2-二氯乙烷 作用下， 以 乙醇 、 二氯甲烷 、 水 为溶剂， 反应 11.33h， 生成 methyl 1-(pyridin-4-ylmethyl)-3,6-dihydro-2H-pyridine-5-carboxylate
  参考文献：
  名称：

  N-Heteroarylmethyl-5-hydroxy-1,2,5,6-tetrahydropyridine-3-carboxylic acid a novel scaffold for the design of uncompetitive α-glucosidase inhibitors

  摘要：

  The enzyme alpha-glucosidase has attracted interest owing to its involvement in the digestive process of carbohydrate, its role in intracellular glycoprotein trafficking, tumorigenesis and viral infection. In this study, several members of a new family of N-heteroarylmethyl substituted azasugars were synthesized and evaluated as alpha-glucosidase inhibitors. We systematically investigated the effect of different N-substituents as well as the role of hydroxyl and carboxylate moieties on the piperidine ring. The compounds N-heteroarylmethyl-5-hydroxy-1,2,5,6-tetrahydropyridine-3-carboxylic acid emerged as potent alpha-glucosidase inhibitors. Unlike Acarbose and other clinically relevant alpha-glucosidase inhibitors, these compounds act through a reversible uncompetitive mechanism of inhibition which make them attractive candidates for drug development. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2013.07.012

文献信息

• N-Heteroarylmethyl-5-hydroxy-1,2,5,6-tetrahydropyridine-3-carboxylic acid a novel scaffold for the design of uncompetitive α-glucosidase inhibitors
  作者：Sha Long、Francesca Romana Stefani、Stefano Biondi、Giancarlo Ghiselli、Mauro Panunzio

  DOI：10.1016/j.bmc.2013.07.012

  日期：2013.9

  The enzyme alpha-glucosidase has attracted interest owing to its involvement in the digestive process of carbohydrate, its role in intracellular glycoprotein trafficking, tumorigenesis and viral infection. In this study, several members of a new family of N-heteroarylmethyl substituted azasugars were synthesized and evaluated as alpha-glucosidase inhibitors. We systematically investigated the effect of different N-substituents as well as the role of hydroxyl and carboxylate moieties on the piperidine ring. The compounds N-heteroarylmethyl-5-hydroxy-1,2,5,6-tetrahydropyridine-3-carboxylic acid emerged as potent alpha-glucosidase inhibitors. Unlike Acarbose and other clinically relevant alpha-glucosidase inhibitors, these compounds act through a reversible uncompetitive mechanism of inhibition which make them attractive candidates for drug development. (C) 2013 Elsevier Ltd. All rights reserved.