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Determination of the specific interaction between palmatine and bovine serum albumin

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Abstract

The binding of palmatine to bovine serum albumin (BSA) was studied under physiological conditions (pH = 7.40) by molecular spectroscopic approach. It was proved that the fluorescence quenching of BSA by palmatine is a result of the formation of palmatine–BSA complex. Binding parameters were determined using the modified Stern–Volmer equation and Scatchard equation, to measure the specific binding between palmatine and BSA. The thermodynamic parameters calculated, ∆G°, ∆H° and ∆S° indicate that the electrostatic interactions play a major role in the palmatine–BSA association. Site marker competitive displacement experiments demonstrated that palmatine binds with specific affinity to site II (subdomain IIIA) of BSA. Furthermore, the specific binding distance r (3.36 nm) was obtained according to fluorescence resonance energy transfer. The results of synchronous fluorescence spectra and UV–Visible absorption spectra show that the conformation of bovine serum albumin has been changed.

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Acknowledgments

The authors gratefully acknowledged financial support of National Natural Science Foundation of China (No. 20803019), Natural Science Foundation of Hubei Province, China (No. 2010CDB00101), and Hubei Normal University Foundation, China (No. 2007F10).

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Authors and Affiliations

  1. Hubei Key Laboratory of Pollutant Analysis & Reuse Technology, Department of Chemistry, Hubei Normal University, Huangshi, 435002, People’s Republic of China

    Yu Ou-Yang, Xiao-Ling Li, Hong Wang, Min Fang & Yan-Jun Hu

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  1. Yu Ou-Yang
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  2. Xiao-Ling Li
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  3. Hong Wang
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  4. Min Fang
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  5. Yan-Jun Hu
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Correspondence to Yan-Jun Hu.

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Ou-Yang, Y., Li, XL., Wang, H. et al. Determination of the specific interaction between palmatine and bovine serum albumin. Mol Biol Rep 39, 5495–5501 (2012). https://doi.org/10.1007/s11033-011-1352-7

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