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Study of the Interaction Between Coenzyme Q10 and Human Serum Albumin: Spectroscopic Approach

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Abstract

UV–vis absorption, fluorescence, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopic methods were employed to reveal the mechanism of the binding between coenzyme Q10 (CoQ10) and human serum albumin (HSA) under simulated physiological conditions (pH = 7.4). The binding parameters were calculated by the fluorescence quenching method. The results demonstrate that the fluorescence quenching of HSA by CoQ10 is mainly static quenching due to the formation of HSA–CoQ10 complexes, and the number of binding sites (n) is equal to 1. The thermodynamic parameters (ΔH 0 = −43.18 kJ·mol−1, ΔS 0 = −47.05 J·mol−1·K−1, ΔG 0 = −29.15 kJ·mol−1) indicate that the enthalpy-driven binding process is favorable, and the main binding forces between CoQ10 and HSA are hydrogen bonds and van der Waals forces. The competitive experiments using different site markers indicate that subdomain IIA (site I) of HSA is the primary binding site for CoQ10. The average binding distance (r) between HSA and CoQ10 is 4.29 nm, which was estimated according to the Förster’s theory of non-radiation energy transfer. In addition, the UV–vis absorption, synchronous fluorescence, three-dimensional fluorescence, 8-anilino-1-naphthalenesulfonic acid fluorescence, CD spectra, and FT-IR spectroscopy data show slight conformational changes of HSA in the presence of CoQ10. These findings provide valuable binding information between HSA and CoQ10, which may be beneficial to pharmacokinetics research and could be used to design the dosage form of CoQ10.

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Acknowledgments

This work was supported by the Program for New Century Excellent Talents in Chinese University (NCET-08-0386), the 863 Program of China (2008AA10Z318, 2012AA06A303, 2013AA102204), the Natural Science Foundation of China (20976125, 31071509, 51173128) and Tianjin (10JCYBJC05100), the Ministry of Science and Technology of China (2012YQ090194), the Beiyang Young Scholar of Tianjin University (2012) and the Program of Introducing Talents of Discipline to Universities of China (Number B06006).

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Authors and Affiliations

  1. School of Life Sciences, Tianjin University, Tianjin, 300072, People’s Republic of China

    Xin Peng

  2. Chemical Engineering Research Center, School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, People’s Republic of China

    Xin Peng, Yinhe Sun, Wei Qi, Rongxin Su & Zhimin He

  3. State Key Laboratory of Chemical Engineering, Tianjin University, Tianjin, 300072, People’s Republic of China

    Wei Qi, Rongxin Su & Zhimin He

  4. Tianjin Key Laboratory of Membrane Science and Desalination Technology, Tianjin University, Tianjin, 300072, People’s Republic of China

    Wei Qi & Rongxin Su

  5. The Co-Innovation Center of Chemistry and Chemical Engineering of Tianjin, Tianjin, People’s Republic of China

    Wei Qi, Rongxin Su & Zhimin He

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Peng, X., Sun, Y., Qi, W. et al. Study of the Interaction Between Coenzyme Q10 and Human Serum Albumin: Spectroscopic Approach. J Solution Chem 43, 585–607 (2014). https://doi.org/10.1007/s10953-014-0146-7

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