Studies on the Interaction Between Triptolide and Bovine Serum Albumin (Bsa) by Spectroscopic and Molecular Modeling Methods

Abstract

Background: Triptolide is a major active constituent isolated from Tripterygiumwilfordii Hook F, a Chinese herbal medicine. This study investigated the intermolecular interaction between triptolide and bovine serum albumin (BSA). Materials and Methods:The fluorescence, circular dichroism (CD) and molecular docking methods were used to investigate the intermolecular interaction between triptolide and BSA. The binding constant, the number of binding sites, binding subdomain and the thermodynamic parameters were measured. Results: The results of this experiment revealed that the intrinsic fluorescence of BSA was effectively quenched by triptolide via static quenching. The experimental results of synchronous fluorescence and CD spectra showed that the conformation of BSA was changed in the presence of triptolide. Conclusion: It indicated that triptolide could spontaneously bind on site II (subdomain IIIA) of BSA mainly via hydrogen bonding interactions and Van der Waals force.

In vitro Interactions of Secnidazole and Its Iron (II), Copper (II) Complexes with Bovine Serum Albumin by Fluorescence Quenching Method

“…Serum albumins (SAs) are the most soluble and plentiful protein present in cardiovascular system, accounts for 50% to 65% of the plasma levels of total protein and involve in the binding and transportation of various biomolecules and drugs (Wang et al, 2016;Cheng et al, 2013). As most of the medications reversibly bind to serum albumins, they are commonly transported in the circulatory system as protein complexes.…”

Interactions of linagliptin, rabeprazole sodium, and their formed complex with bovine serum albumin: Computational docking and fluorescence spectroscopic methods

“…In living organisms, protein plays a vital role by participating in various biological processes. Serum albumins (SAs), which account for 50%–65% of the total protein, are the highest soluble and affluent protein present in the circulatory system, involved in the binding, and act as carriers of ligands or responsible for the movement of various drugs and biomolecules 1,2 . Since most of the administered medications reversibly interact with serum proteins, they are transported in the systemic circulation primarily as protein complexes.…”

“…Serum albumins (SAs), which account for 50%–65% of the total protein, are the highest soluble and affluent protein present in the circulatory system, involved in the binding, and act as carriers of ligands or responsible for the movement of various drugs and biomolecules. 1 , 2 Since most of the administered medications reversibly interact with serum proteins, they are transported in the systemic circulation primarily as protein complexes. In this manner, drug–protein interaction also has immense biological importance and has been found to play a critical role in pharmacology.…”

Transition Metal Chelation Augments the Half-life of Secnidazole: Molecular Docking and Fluorescence Spectroscopic Approaches

“…Serum albumins play a vital role in various biological processes in living organisms, which are the most affluent and show the highest solubility present in the cardiovascular system. These significant proteins account for 50-65 % of the total protein's plasma levels, and act as transporters or carriers for various drugs or biomolecules [2,3]. Serum albumins are the proteins in which most of the administered drugs bind extensively and reversibly and these drugs are transported mainly as protein complexes.…”