期刊
JOURNAL OF MOLECULAR RECOGNITION
卷 32, 期 1, 页码 -出版社
WILEY
DOI: 10.1002/jmr.2758
关键词
bisphenol analogues; hemoglobin; molecular docking; spectroscopy
资金
- Natural Science Foundation of Shandong Province [ZR2016YL013]
- Science and Technology Development Plan of Shandong Province [2014GSF117027]
- Research Fund for the Doctoral Program of Higher Education [20130131110016, 708058]
- Cultivation Fund of the Key Scientific and Technical Innovation Project
- NSFC [21777088, 21477067, 21277081]
- Ministry of Education of China [20130131110016, 708058]
Bisphenol F (BPF), bisphenol S (BPS), and bisphenol B (BPB) have been extensively used in food packaging, plasticizer, and paper products, causing more concern about their biosafety. The mechanism of these bisphenols' toxicity was investigated by determining diverse effects of them on common protein bovine hemoglobin (BHb). The effects at the molecular level were determined by ultraviolet-visible, circular dichroism, resonance light scattering, fluorescence spectroscopy, and molecular docking. The irreversible cross-linking results of bisphenols and BHb demonstrate that hydrogen (H) bonding and hydrophobic forces play major roles in the interaction. Both BPF and BPS decreased the amount of alpha-helix, leading to the loosening of protein skeleton while BPB made little change. In the loose structure, BPF exposed the internal amino acids to a hydrophobic environment and BPS (above 10 mu M) obviously quenched characteristic fluorescence. The variant effects of BPF, BPS, and BPB may arise from different structural formula. Accordingly, BPB could be used as a better substitute for bisphenol A, and it is necessary to control the concentration of BPS and BPF below 10 mu M in application. This study provided important basis for application of BPB and safe use of bisphenol analogues in industry.
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