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The characterization of 1-(4-bromophenyl)-5-phenyl-1H-1,2,3-triazole on acute toxicity, antimicrobial activities, photophysical property, and binding to two globular proteins

文献类型： 外文期刊

作者： Liu, He 1 ; Lin, Qiang 1 ; Xie, Yixian 2 ; Shu, Huoming; Li, Bo 1 ; Gao, Ge 1 ; Xiao, Kai 1 ; Yao, Xiaojun; Dong, Runc 1 ;

作者机构： 1.Hainan Normal Univ, Minist Educ, Key Lab Trop Med Plant Chem, Haikou 571158, Hainan, Peoples R China

2.Chin

关键词： BPT;Acute toxicity;Antimicrobial activities;HIg;BHg;Binding

期刊名称：JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY （ 影响因子：6.252； 五年影响因子：5.375 ）

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收录情况： SCI

摘要： 1-(4-Bromophenyl)-5-phenyl-1H-1,2,3-triazole (BPT) was a newly synthesized compound. The acute toxicities of BPT to mice by intragastric administration have been determined and the result indicates that the intragastric administration of BPT did not produce any significant toxic effect on Kunming strain mice. It is also evaluated for the antimicrobial activity of BPT against three kinds of plant mycoplasma, Fusarium Wilt (race 4), Colletotrichum gloeosporioides Penz. and Xanthomonas oryzae by different method in vitro. The compound exhibited distinct inhibitory activities against Fusarium Wilt (race 4) and Colletotrichum gloeosporioides Penz. by mycelium growth rate test and the values of EC50 were 2934 and 12.53 mu g/mL respectively. And BPT had also the most potent inhibitory activities against Xanthomonas oryzae when compared with that of control drugs by the agar well diffusion method. In addition, the structural and photophysical properties of BPT including ionization energy, electron affinities, and theoretical spectrum was studied by quantum-chemical methods. Then the interaction of BPT with two kinds of globular proteins, human immunoglobulin (HIg) and bovine hemoglobin (BHg) was investigated by using UV-vis absorption spectra, synchronous fluorescence, 3D fluorescence spectra, and fluorescence titration in combination with molecular modeling. UV-vis absorption, 3D and synchronous fluorescence measurements show that BPT has influence on the microenvironment surrounding HIg or BHg in aqueous solution and the fluorescence experiments show that BPT quenches the fluorescence intensity of HIg or BHg through a static mechanism. The binding parameters including the binding constants, the number of binding site and average binding distance between BPT and HIg or BHg at different temperatures were calculated. The thermodynamic parameters suggest that the hydrophobic interaction is the predominant intermolecular forces in stabilizing the BPT-HIg or BPT-BHg complex. Molecular docking was performed to reveal that the BPT moiety binds to the hydrophobic cavity of HIg or BHg and they are in good agreement with the spectroscopic measurements. (C) 2016 Elsevier B.V. All rights reserved.

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