Research Article Open Access

The Effect of Trilobatin on Bovine Serum Albumin: Interaction Mechanism and Molecular Docking

Yuhan Zhai1, Yuqing Zhang2, Yaping Li2, Haifang Xiao2 and Yuanda Song2
  • 1 Department of Food Science and Engineering, Colin Ratledge Center for Microbial Lipids, School of Agricultural Engineering and Food Science, Shandong University of Technology, 266 Xincun West Road, Zibo, China
  • 2 Department of Food Science and Engineering, Colin Ratledge Center for Microbial Lipids, School of Agricultural Engineering and Food Science, Shandong University of Technology, 266 Xincun West Road, Zibo, China

Abstract

Understanding the transport and distribution of small molecules in vivo is aided by studying their interactions with proteins. As a natural sweetener, trilobatin possesses several biological activities. However, uncertainty surrounds the trilobatin and Bovine Serum Albumin (BSA) interaction mechanism. In this study, the binding types, number of binding sites and binding constants of trilobatin interaction with BSA were studied by fluorescence spectrometry. The effect of trilobatin on the spatial conformation of BSA was investigated using FT-IR, fluorescence and UV-V is absorption spectra. Moreover, the molecular docking method was employed to research the exact binding model of trilobatin and BSA. Findings from this investigation demonstrated that static quenching was the method by which trilobatin suppressed the fluorescence of BSA. The binding constants Ka of trilobatin and BSA at 298, 304 and 310 K were 2.23×104, 3.06×104 and 6.39×104 moL/L, respectively and only a single site of BSA was bound to trilobatin. According to the discoveries of molecular simulation and thermodynamic analysis, the predominant forces between trilobatin and BSA were hydrogen bond and hydrophobic force (ΔH° >0 and ΔS° >0). Trilobatin and BSA had an endothermic, entropy-driven reaction during their binding contact (ΔG° >0). Additionally, non-radiative energy transfer took place among trilobatin and BSA because their binding distance was smaller than 7 nm. Moreover, trilobatin altered the microenvironment and conformation of BSA and formed the non-fluorescent ground state complex. Important data supporting trilobatin’s availability and distribution were supplied by this investigation.

American Journal of Biochemistry and Biotechnology
Volume 20 No. 1, 2024, 33-42

DOI: https://doi.org/10.3844/ajbbsp.2024.33.42

Submitted On: 1 July 2023 Published On: 29 March 2024

How to Cite: Zhai, Y., Zhang, Y., Li, Y., Xiao, H. & Song, Y. (2024). The Effect of Trilobatin on Bovine Serum Albumin: Interaction Mechanism and Molecular Docking. American Journal of Biochemistry and Biotechnology, 20(1), 33-42. https://doi.org/10.3844/ajbbsp.2024.33.42

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Keywords

  • Trilobatin
  • Bovine Serum Albumin (BSA)
  • Interaction
  • Spectroscopic Method and Molecular Docking