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Study of caffeine binding to human serum albumin using optical spectroscopic methods

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Abstract

The binding of caffeine to human serum albumin (HSA) under physiological conditions has been studied by the methods of fluorescence, UV-vis absorbance and circular dichroism (CD) spectroscopy. The mechanism of quenching of HSA fluorescence by caffeine was shown to involve a dynamic quenching procedure. The number of binding sites n and apparent binding constant K b were measured by the fluorescence quenching method and the thermodynamic parameters ΔH, ΔG, ΔS were calculated. The results indicate that the binding is mainly enthalpy-driven, with van der Waals interactions and hydrogen bonding playing major roles in the reaction. The distance r between donor (HSA) and acceptor (caffeine) was obtained according to the Förster theory of non-radiative energy transfer. Synchronous fluorescence, CD and three-dimensional fluorescence spectroscopy showed that the microenvironment and conformation of HSA were altered during the reaction.

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Authors and Affiliations

  1. College of Chemistry & Chemical Engineering, Hubei University, Wuhan, 430062, China

    Qiong Wu

  2. State Key Laboratory of Virology & College of Chemistry and Molecular Sciences, Wuhan University, Wuhan, 430072, China

    Qiong Wu, YanJun Hu & Yi Liu

  3. Key Laboratory for Oral Biomedical Engineering of MOE & School of Stomatology, Wuhan University, Wuhan, 430072, China

    ChaoHong Li

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  1. Qiong Wu
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  2. ChaoHong Li
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  3. YanJun Hu
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  4. Yi Liu
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Correspondence to Yi Liu.

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Wu, Q., Li, C., Hu, Y. et al. Study of caffeine binding to human serum albumin using optical spectroscopic methods. Sci. China Ser. B-Chem. 52, 2205–2212 (2009). https://doi.org/10.1007/s11426-009-0114-z

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  • DOI: https://doi.org/10.1007/s11426-009-0114-z

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