3-benzothiazol-2-yl-7-diethylamino-4-(1H-tetrazol-5-yl)-chromen-2-one | 94594-17-9

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 香豆素及其衍生物
• 英文名称: 3-benzothiazol-2-yl-7-diethylamino-4-(1H-tetrazol-5-yl)-chromen-2-one
• 英文别名: 3-(1,3-benzothiazol-2-yl)-7-(diethylamino)-4-(2H-tetrazol-5-yl)chromen-2-one
• CAS: 94594-17-9
• 化学式: C₂₁H₁₈N₆O₂S
• 分子量: 418.479
• InChiKey: NRGLYIURWRJMFT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  30
• 可旋转键数：
  5
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  125
• 氢给体数：
  1
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  3-(2-苯并噻唑基)-7-(二乙氨基)-2-氧代-2H-1-苯并吡喃-4-腈 在 sodium azide 、 zinc dibromide 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 48.0h， 以76%的产率得到3-benzothiazol-2-yl-7-diethylamino-4-(1H-tetrazol-5-yl)-chromen-2-one
  参考文献：
  名称：

  Inhibition of amyloid-β aggregation by coumarin analogs can be manipulated by functionalization of the aromatic center

  摘要：

  Aggregation of the amyloid-beta protein (A beta) plays a pathogenic role in the progression of Alzheimer's disease, and small molecules that attenuate A beta aggregation have been identified toward a therapeutic strategy that targets the disease's underlying cause. Compounds containing aromatic structures have been repeatedly reported as effective inhibitors of A beta aggregation, but the functional groups that influence inhibition by these aromatic centers have been less frequently explored. The current study identifies analogs of naturally occurring coumarin as novel inhibitors of A beta aggregation. Derivatization of the coumarin structure is shown to affect inhibitory capabilities and to influence the point at which an inhibitor intervenes within the nucleation dependent A beta aggregation pathway. In particular, functional groups found within amyloid binding dyes, such as benzothiazole and triazole, can improve inhibition efficacy. Furthermore, inhibitor intervention at early or late stages within the amyloid aggregation pathway is shown to correlate with the ability of these functional groups to recognize and bind amyloid species that appear either early or late within the aggregation pathway. These results demonstrate that functionalization of small aromatic molecules with recognition elements can be used in the rational design of A beta aggregation inhibitors to not only enhance inhibition but to also manipulate the inhibition mechanism. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2011.03.010

文献信息

• Inhibition of amyloid-β aggregation by coumarin analogs can be manipulated by functionalization of the aromatic center
  作者：Deborah D. Soto-Ortega、Brandon P. Murphy、Francisco J. Gonzalez-Velasquez、Kelly A. Wilson、Fang Xie、Qian Wang、Melissa A. Moss

  DOI：10.1016/j.bmc.2011.03.010

  日期：2011.4

  Aggregation of the amyloid-beta protein (A beta) plays a pathogenic role in the progression of Alzheimer's disease, and small molecules that attenuate A beta aggregation have been identified toward a therapeutic strategy that targets the disease's underlying cause. Compounds containing aromatic structures have been repeatedly reported as effective inhibitors of A beta aggregation, but the functional groups that influence inhibition by these aromatic centers have been less frequently explored. The current study identifies analogs of naturally occurring coumarin as novel inhibitors of A beta aggregation. Derivatization of the coumarin structure is shown to affect inhibitory capabilities and to influence the point at which an inhibitor intervenes within the nucleation dependent A beta aggregation pathway. In particular, functional groups found within amyloid binding dyes, such as benzothiazole and triazole, can improve inhibition efficacy. Furthermore, inhibitor intervention at early or late stages within the amyloid aggregation pathway is shown to correlate with the ability of these functional groups to recognize and bind amyloid species that appear either early or late within the aggregation pathway. These results demonstrate that functionalization of small aromatic molecules with recognition elements can be used in the rational design of A beta aggregation inhibitors to not only enhance inhibition but to also manipulate the inhibition mechanism. (C) 2011 Elsevier Ltd. All rights reserved.