Investigation of the interaction of a polyamine-modified flavonoid with bovine serum albumin (BSA) by spectroscopic methods and molecular simulation.

Journal of Photochemistry and Photobiology. B, Biology
Zhiyong TianZhihui Tian

Abstract

The interaction between BSA and compound 1 was studied by UV-vis, fluorescence and circular dichroism spectroscopy under physiological conditions (pH = 7.4). Molecular docking and molecular dynamics analyses were also performed. The results showed that compound 1 could bind to BSA. When compound 1 bound to BSA, there were a series of changes in the spectral properties of BSA, which were an enhancement effect of the UV-Vis spectrum of BSA, fluorescence quenching and a weak conformational change in the CD spectrum. The results of the fluorescence experiments at 298, 303 and 310 K showed that fluorescence quenching caused by the addition of compound 1 to BSA was generally static quenching accompanied by a dynamic quenching process, which was shown by the quenching constants of 2.010 × 104 L∙M-1, 1.850 × 104 L∙M-1, and 1.970 × 104 L∙M-1 at the three different temperatures, respectively. From the obtained binding constants and thermodynamic parameters, it was found that hydrophobic forces played an important role in the binding process of 1 to BSA. The results of synchronous fluorescence and three-dimensional fluorescence showed that compound 1 caused a weak conformational change in BSA. Docking results showed that compound 1 was lo...Continue Reading

Citations

May 1, 2021·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Qiaomei SunHui Li
Jun 29, 2021·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Shi-Yu LiuGuan-Hu Bao

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