Insights into the binding interaction mechanism of 12,12-dihydrochromeno[2,3-c]isoquinolin-5-amine in bovine serum albumin and prostaglandin H2 synthase-1: A biophysical approach

The current study investigates the newly synthesized 12,12-dihydrochromeno[2,3-c]isoquinolin-5-amine (drug) molecule binding interaction mechanism with bovine serum albumin (BSA) and prostaglandin H2 synthase-1(PTGS1), using biophysical techniques. The emission spectroscopy shows a possibility of static quenching mechanism between BSA and drug complex and the thermo dynamical parameter result suggests hydrophobic interactions between BSA and drug. The excitation emission matrix and circular dichroism analysis concludes the presence of drug in BSA molecule. Molecular docking studies for the complex of drug shows good binding affinity in BSA, PTGS1 complex system and the BSA-drug computational docking score is almost in the same order of experimentally determined values. The molecular dynamics simulations were performed to understand drug binding stability in BSA, PTGS1 complex system for 50 ns. The density functional theory calculations were also performed to understand the intermolecular interaction mechanism of free drug and drug in BSA, PTGS1 binding active site environment. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

The study investigated the binding interaction mechanism of a newly synthesized drug molecule with proteins BSA and PTGS1 using biophysical techniques, revealing static quenching and hydrophobic interactions as possible mechanisms. Molecular docking studies showed good binding affinity between the drug and BSA, PTGS1 complex, supported by molecular dynamics simulations. Density functional theory calculations provided insights into the intermolecular interaction mechanism of the drug in the binding active site environment of BSA and PTGS1.