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Investigation of Interaction Between Ozagrel and Human Serum Albumin by Spectroscopic and Electrochemical Methods

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Journal of Applied Spectroscopy Aims and scope

The interaction between ozagrel and human serum albumin (HSA) was investigated by fl uorescence spectroscopy, UV-Vis absorption spectroscopy, cyclic voltammetry (CV), differential pulse voltammetry (DPV), and Fourier transform infrared spectroscopy (FTIR) under simulative physiological conditions. The results of CV, DPV and fl uorescence titration revealed that ozagrel bound to HSA. The enthalpy change (ΔH) and the entropy change (ΔS) were derived to be positive values, indicating that the hydrophobic force played the main role in the binding of ozagrel with HSA. The binding distance between ozagrel and HSA was 1.75 nm. Upon binding with ozagrel, the conformation and the secondary structure of HSA molecules were changed. The percentage of α-helix and β-sheet structures decreased by 7.25% and 4.58%, respectively, while the percentage of a β-turn structure increased by 2.67%. The effect of common ions on the binding of ozagrel with HSA was also examined. This study will give an insight into the evaluation of the drug’s stabi-lity during transport and its releasing effi ciency at the target site under simulative physiological conditions.

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Authors and Affiliations

  1. College of Pharmacy, Shanxi Medical University, Taiyuan, 030001, China

    S. Li, Li Wang, J. Hao, L. Wang, Y.-J. Tong, Z.-Q. Fu & A.-P. Zhang

  2. Shanxi Eye Hospital, Taiyuan, 030002, PR China

    Li Wang

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  1. S. Li
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  2. Li Wang
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  3. J. Hao
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  4. L. Wang
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  5. Y.-J. Tong
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  7. A.-P. Zhang
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Correspondence to A.-P. Zhang.

Additional information

Abstract of article is published in Zhurnal Prikladnoi Spektroskopii, Vol. 83, No. 6, p. 1008, November–December, 2016.

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Li, S., Wang, L., Hao, J. et al. Investigation of Interaction Between Ozagrel and Human Serum Albumin by Spectroscopic and Electrochemical Methods. J Appl Spectrosc 83, 1076–1083 (2017). https://doi.org/10.1007/s10812-017-0410-x

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  • DOI: https://doi.org/10.1007/s10812-017-0410-x

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