Study of the interaction between mercury (II) and bovine serum albumin by spectroscopic methods |
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| Affiliation: | 1. Liaoning Medical University, Jinzhou 121001, PR China;2. Key Laboratory of Environment and Health, Ministry of Education & Ministry of Environmental Protection, and State Key Laboratory of Environmental Health (Incubating) School of Public Health, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, PR China;1. Department of Biochemistry and Biotechnology, Precarpathian National University named after Vassyl Stefanyk, 57 Shevchenko Str., Ivano-Frankivsk 76025, Ukraine;2. Institute of Biochemistry, Carleton University, 1125 Colonel By Drive, Ottawa, Ontario K1S 5B6, Canada;1. Radiation Biotechnology Laboratory, Department of Radiation Biosciences, Institute of Nuclear and Allied Sciences, Delhi 110054, India;2. Department of Biochemistry, Faculty of Science, Jamia Hamdard, Delhi 110062, India;1. Department of Biochemistry, School of Medicine, Nantong University, 19 Qi Xiu Rode, 226001 Nantong, China;2. Department of Biosystem Engineering, College of Biosystem Engineering and Food Science, Zhejiang University, 388 Yu Hang Tang Road, 310058 Hangzhou, China;3. Department of Biochemistry and Genetics, School of Medicine, Zhejiang University, 388 Yu Hang Tang Road, 310058 Hangzhou, China;1. School of Public Health, Taishan Medical University, Taian 271000, China;2. School of Public Health, Shandong University, Jinan 250012, China;3. College of Animal Science & Veterinary Medicine, Guangxi University, Nanning 530004, China;4. Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;5. Ruijin Hospital, Shanghai Jiao Tong University, Shanghai 200025, China |
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| Abstract: | Mercury is a significant environmental pollutant that originates from industry. Mercury will bind with albumin and destroy biological functions in humans if it enters the blood. In this paper, the interaction between mercury (II) and bovine serum albumin (BSA) was investigated in vitro by fluorescence, UV–Vis absorption and circular dichroism (CD) under simulated physiological conditions. This study proves that the probable quenching mechanism of BSA by mercury (II) was mainly static quenching due to the formation of a mercury (II)–BSA complex. The quenching constant Ka and the corresponding thermodynamic parameters (ΔH, ΔS and ΔG) at four different temperatures were calculated by a modified Stern–Volmer equation and the van’t Hoff equation, respectively. The results revealed that the interaction between mercury (II) and BSA was mainly enthalpy-driven and that hydrogen bonding and van der Waals forces played a major role in the reaction. The obtained data for binding sites of n approximately equal to 1 indicated that there was a single class of binding site for the BSA with mercury (II). The value of the distance r (3.55 nm), determined by Föster's non-radioactive energy transfer theory, suggested that the energy transfer from BSA to mercury (II) occurred with a high probability. The conformational investigation from synchronous fluorescence, CD spectroscopy and three-dimensional fluorescence showed that the presence of mercury (II) resulted in micro-environmental and conformational changes of the BSA molecules, which may be responsible for the toxicity of mercury (II) in vivo. |
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| Keywords: | Bovine serum albumin (BSA) Mercury Fluorescence spectroscopy Thermodynamic parameter Circular dichroism (CD) Three-dimensional fluorescence spectra |
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