1-(1-羟基-2-萘基)-3-苯基丙烷-1,3-二酮 | 63450-45-3

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 直链 1,3-二芳基丙烷
• 中文名称: 1-(1-羟基-2-萘基)-3-苯基丙烷-1,3-二酮
• 英文名称: 1-(1-hydroxynaphthalen-2-yl)-3-phenylpropane-1,3-dione
• 英文别名: 1-hydroxy-2-naphthoylacetophenone；1-(1-hydroxy-[2]naphthyl)-3-phenyl-propane-1,3-dione；1-(1-Hydroxy-[2]naphthyl)-3-phenyl-propan-1,3-dion；1,3-Propanedione, 1-(1-hydroxy-2-naphthalenyl)-3-phenyl-
• CAS: 63450-45-3
• 化学式: C₁₉H₁₄O₃
• 分子量: 290.318
• InChiKey: SIVIDNLTOXSUIX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.6
• 重原子数：
  22
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.05
• 拓扑面积：
  54.4
• 氢给体数：
  1
• 氢受体数：
  3

安全信息

• 海关编码：
  2914501900

反应信息

• 作为反应物：
  描述：

  1-(1-羟基-2-萘基)-3-苯基丙烷-1,3-二酮 在 硫酸 作用下， 以 溶剂黄146 为溶剂， 以72%的产率得到α-萘黄酮
  参考文献：
  名称：

  Benzoflavone derivatives as potent antihyperuricemic agents

  摘要：

  苯并黄酮衍生物经过合理设计、合成并针对黄嘌呤氧化酶进行评估，以检测它们的抗高尿酸作用，使用体外和体内方法。

  DOI：

  10.1039/c8md00512e
• 作为产物：
  描述：

  2-乙酰基-1-萘酚 在 吡啶 、 potassium hydroxide 作用下， 以 吡啶 为溶剂， 反应 1.5h， 生成 1-(1-羟基-2-萘基)-3-苯基丙烷-1,3-二酮
  参考文献：
  名称：

  Benzoflavone derivatives as potent antihyperuricemic agents

  摘要：

  苯并黄酮衍生物经过合理设计、合成并针对黄嘌呤氧化酶进行评估，以检测它们的抗高尿酸作用，使用体外和体内方法。

  DOI：

  10.1039/c8md00512e

文献信息

• Rh(III)‐Catalyzed Aldehydic C−H Functionalization Reaction between Salicylaldehydes and Sulfoxonium Ylides
  作者：Guo‐Dong Xu、Kenneth L. Huang、Zhi‐Zhen Huang

  DOI：10.1002/adsc.201900276

  日期：2019.7.11

  A novel aldehydic C−H functionalization reaction between salicylaldehydes and sulfoxonium ylides has been developed under rhodium(III) catalysis, affording coupling products in moderate to good yields. A plausible mechanism involving aldehydic C(sp2)−H activation by rhodium(III) and rhodium(III) catalyzed carbene insertion is also proposed. It was also found that the aldehydic C−H functionalization

  在铑（III）催化下，开发了水杨醛与亚磺酰之间的新型醛C-H官能化反应，可提供中等至良好收率的偶联产物。还提出了一种可能的机理，该机理涉及通过铑（III）和铑（III）催化的卡宾插入而使醛类的C（sp 2）-H活化。还发现醛化的CH功能化然后脱水环化能够在一锅中产生类黄酮。
• Benzoflavone activators of the cystic fibrosis transmembrane conductance regulator: towards a pharmacophore model for the nucleotide-binding domain
  作者：Mark F Springsteel、Luis J.V Galietta、Tonghui Ma、Kolbot By、Gideon O Berger、Hong Yang、Christopher W Dicus、Wonken Choung、Chao Quan、Anang A Shelat、R.Kiplin Guy、A.S Verkman、Mark J Kurth、Michael H Nantz

  DOI：10.1016/s0968-0896(03)00435-8

  日期：2003.9

  using cell-based assays, of a series of benzoflavone analogues to examine structure-activity relationships and to identify compounds having greater potency for activation of both wild type CFTR and a mutant CFTR (G551D-CFTR) that causes cystic fibrosis in some human subjects. Using UCCF-029 as a structural guide, a panel of 77 flavonoid analogues was prepared. Analysis of the panel in FRT cells indicated

  我们以前对黄酮类化合物和相关杂环的筛选具有激活囊性纤维化跨膜电导调节剂（CFTR）氯化物通道的能力，这表明UCCF-029是一种7,8-苯并黄酮，是一种有效的活化剂。在本研究中，我们描述了使用基于细胞的分析方法对一系列苯并黄酮类似物进行合成和评估，以检查其结构活性关系，并鉴定出对野生型CFTR和突变型CFTR（G551D -CFTR）在某些人类受试者中引起囊性纤维化。使用UCCF-029作为结构指导，制备了77种类黄酮类似物。对FRT细胞中面板的分析表明，黄酮A环在7,8位的苯环显着提高了化合物活性和几种类黄酮的效力。在3或4位上引入B环吡啶基氮也可提高CFTR活性，但这种结构修饰的影响不如苯甲环化均匀。最有效的新类似物UCCF-339以1.7 microM的K（d）激活了野生型CFTR，它比以前最有效的CFTR类黄酮活化剂芹菜素具有更高的活性。苯并黄酮类化合物中的几种化合物也可以活化G5
• 387. Synthetical experiments in the chromone group. Part XIV. The action of sodamide on 1-acyloxy-2-acetonaphthones
  作者：Harbhajan S. Mahal、Krishnasami Venkataraman

  DOI：10.1039/jr9340001767

  日期：——
• Benzoflavones as cholesterol esterase inhibitors: Synthesis, biological evaluation and docking studies
  作者：Harbinder Singh、Jatinder Vir Singh、Manish K. Gupta、Palwinder Singh、Sahil Sharma、Kunal Nepali、Preet Mohinder S. Bedi

  DOI：10.1016/j.bmcl.2017.01.020

  日期：2017.2

  A library of forty 7,8-benzoflavone derivatives was synthesized and evaluated for their inhibitory potential against cholesterol esterase (CEase). Among all the synthesized compounds seven benzoflavone derivatives (A-7, A-8, A-10, A-11, A-12, A-13, A-15) exhibited significant inhibition against CEase in in vitro enzymatic assay. Compound A-12 showed the most promising activity with IC50 value of 0.78 nM against cholesterol esterase. Enzyme kinetic studies carried out for A-12, revealed its mixed-type inhibition approach. Molecular protein ligand docking studies were also performed to figure out the key binding interactions of A-12 with the amino acid residues of the enzyme's active site. The A-12 fits well at the catalytic site and is stabilized by hydrophobic interactions. It completely blocks the catalytic assembly of CEase and prevents it to participate in ester hydrolysis mechanism. The favorable binding conformation of A-12 suggests its prevailing role as CEase inhibitor. (C) 2017 Elsevier Ltd. All rights reserved.
• Garg, S.; Ishar, M. P. S.; Sarin, R., Indian Journal of Chemistry - Section B Organic and Medicinal Chemistry, 1994, vol. 33, # 12, p. 1123 - 1128
  作者：Garg, S.、Ishar, M. P. S.、Sarin, R.、Gandhi, R. P.

  DOI：——

  日期：——