Binding of β-casein with fluvastatin and pitavastatin Scientific paper

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Published: Sep 16, 2022
Updated: 16.09.2022
DOI: https://doi.org/10.2298/JSC220606067D
Keywords:
milk protein statin molecular modeling spectroscopy

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Hamid Dezhampanah
Laboratory of Physical Chemistry, Department of Chemistry, Faculty of Science, University of Guilan P.O. Box 1914, Rasht 0098, Iran
https://orcid.org/0000-0002-4378-2722
Omideh Rajabi Miandehi
Laboratory of Physical Chemistry, Department of Chemistry, Faculty of Science, University of Guilan P.O. Box 1914, Rasht 0098, Iran
https://orcid.org/0000-0003-2839-1704

Abstract

In this work, the binding interaction of fluvastatin (FLU) and pit-av­astatin (PIT) with bovine β-casein (β-CN) were performed under physiological conditions (pH 7.2) by fluorescence emission spectroscopy, synchronous fluor­escence spectroscopy, Fourier transform infrared spectroscopy (FTIR) and molecular docking methods. Due to the formation of FLU-β-CN and PIT-β-CN complexes, the intrinsic fluorescence of β-CN was quenched. The number of bound FLU and PIT per protein molecule (n) were about 1, also the binding constant of FLU-β-CN and PIT-β-CN complexes were 7.96×104 and 3.44×104 M-1 at 298 K, respectively. This result suggests that the binding affinity of FLU to β-CN was higher than that for PIT. Molecular modelling showed different binding sites for FLU and PIT on β-CN. All these experimental results suggest that β-CN can be used as a carrier protein which delivers FLU and PIT based drugs to target molecules.

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How to Cite
[1]
H. Dezhampanah and O. Rajabi Miandehi, “Binding of β-casein with fluvastatin and pitavastatin: Scientific paper”, J. Serb. Chem. Soc., vol. 87, no. 11, pp. 1273–1284, Sep. 2022.
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Vol. 87 No. 11 (2022)
Section
Theoretical Chemistry
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