15116-13-9Relevant articles and documents
Determining Essential Requirements for Fluorophore Selection in Various Fluorescence Applications Taking Advantage of Diverse Structure-Fluorescence Information of Chromone Derivatives
Chen, Yikun,Gao, Yongxin,He, Yujun,Zhang, Gang,Wen, Hui,Wang, Yuchen,Wu, Qin-Pei,Cui, Huaqing
, p. 1001 - 1017 (2021/01/09)
Herein, we report our work exploring the essential requirements for fluorophore selection during the development of various fluorescence applications. We assembled a library of chromone-derived fluorophores with diverse structure-fluorescence properties, which allowed us to choose the fluorophore pairs with similar structures but differing fluorescence properties and compared the performance of the selected fluorophore pairs in three types of commonly used fluorescence applications. We found that the selection standard of a suitable fluorophore is variable depending on the application. (1) In fluorescence imaging, fluorophores with strong and constant fluorescence under various conditions, such as a large pH range, are preferred. Notably, (2) in the detection of bioactive species, fluorophores with relatively lower fluorescence quantum yield favor the detection sensitivity. Furthermore, (3) in enzymatic assays employing fluorescence, the key parameter is the binding affinity between the fluorophore and the enzyme.
Exploring efficacy of natural-derived acetylphenol scaffold inhibitors for α-glucosidase: Synthesis, in vitro and in vivo biochemical studies
Dong, Qingjian,Li, Ding,Liu, Ting,Liu, Zhigang,Yu, Xiao,Zhang, Fan
supporting information, (2020/10/02)
The discovery of novel α-glucosidase inhibitors and anti-diabetic candidates from natural or natural-derived products represents an attractive therapeutic option. Here, a collection of acetylphenol analogues derived from paeonol and acetophenone were synthesized and evaluated for their α-glucosidase inhibitory activity. Most of derivatives, such as 9a–9e, 9i, 9m–9n and 11d–1e, (IC50 = 0.57 ± 0.01 μM to 8.45 ± 0.57 μM), exhibited higher inhibitory activity than the parent natural products and were by far more potent than the antidiabetic drug acarbose (IC50 = 57.01 ± 0.03 μM). Among these, 9e and 11d showed the most potent activity in a non-competitive manner. The binding processes between the two most potent compounds and α-glucosidase were spontaneous. Hydrophobic interactions were the main forces for the formation and stabilization of the enzyme - acetylphenol scaffold inhibitor complex, and induced the topography image changes and aggregation of α-glucosidase. In addition, everted intestinal sleeves in vitro and the maltose loading test in vivo further demonstrated the α-glucosidase inhibition of the two compounds, and our findings proved that they have significant postprandial hypoglycemic effects.
Application of paeonol derivatives with vasodilator activity
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Paragraph 0028; 0033; 0034, (2018/12/13)
The invention provides application of paeonol derivatives with vasodilator activity. The method comprises the following steps: carrying out a methylation reaction of 2,4-dihydroxyphenylpentanone underalkaline conditions, sequentially extracting and drying