Protein binding of 4-hydroxybenzoic acid and 4-hydroxy-3-methoxyben-zoic acid to human serum albumin and their anti-proliferation on doxorubicin-sensitive and doxorubicin-resistant leukemia cells

被引:8
|
作者
Myint, Ohnmar [1 ,2 ,3 ]
Wattanapongpitak, Sakornniya [1 ,2 ]
Supawat, Benjamaporn [1 ,2 ]
Kothan, Suchart [1 ,2 ]
Udomtanakunchai, Chatchanok [1 ,2 ]
Tima, Singkome [4 ]
Tungjai, Montree [1 ,2 ]
机构
[1] Chiang Mai Univ, Fac Associated Med Sci, Dept Radiol Technol, Chiang Mai 50200, Thailand
[2] Chiang Mai Univ, Fac Associated Med Sci, Dept Radiol Technol, Ctr Radiat Res & Med Imaging, Chiang Mai, Thailand
[3] Chiang Mai Univ, Fac Associated Med Sci, PhD Degree Program Biomed Sci, Chiang Mai, Thailand
[4] Chiang Mai Univ, Fac Associated Med Sci, Dept Med Technol, Chiang Mai, Thailand
关键词
Fluorescence quenching; 4-Hydroxybenzoic acid; Vanillic acid; Cancer; Phenolic acid; PHENOLIC-ACIDS; FLAVONOIDS; POLYPHENOL; ABSORPTION;
D O I
10.1016/j.toxrep.2021.07.001
中图分类号
R99 [毒物学(毒理学)];
学科分类号
100405 ;
摘要
4-Hydroxybenzoic acids (4-HBA) and 4-hydroxy-3-methoxybenzoic acid (Vanillic acid, VA) have exhibited several pharmacological activities. Generally, the biological activities of compounds are highly involved in the interaction between protein and compounds in blood plasma. The objective was to investigate the interaction of 4-HBA or VA with human serum albumin (HSA) and their anti-proliferation properties on doxorubicin-sensitive K562 and doxorubicin-resistant K562/Dox leukemia cells. The protein binding of 4-HBA or VA to HSA was investigated using fluorescence quenching at temperatures of 298 and 310 Kelvin (K) under the pH of 6.0, 7.4, and 8.0 conditions. The effect of 4-HBA and VA on anti-proliferation was also studied on doxorubicin-sensitive K562 and doxorubicin-resistant K562/Dox leukemia cells using resazurin assay. The results showed that 4-HBA and VA could interact with HSA. The fluorescence quenching process in HSA-4-HBA system might be attributed to static quenching mechanism. In contrast, a dynamic quenching mechanism might be mainly involved in the fluorescence quenching process in the HSA-VA system. Thermodynamic data suggested that the spontaneous interaction between HSA and 4-HBA or VA had occurred in the system and it also indicated that hydrogen bonds and Van der Waals forces contributed to the binding of HSA to 4-HBA or VA. In addition, 4-HBA and VA decreased K562 and K562/Dox cells viability in a dose- and time-dependence manner. In conclusions, the 4-HBA and VA could interact with HSA. In addition, the 4-HBA and VA decreased in cell viability for both doxorubicin-sensitive K562 and doxorubicin-resistant K562/Dox leukemia cells in a dose- and time-dependence manner. Therefore, these current studies could provide useful information about the nature of 4-HBA or VA binding to protein HSA and their anticancer activities in both of these types of leukemia cells. The cell death mechanisms should be investigated through future study.
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页码:1381 / 1388
页数:8
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