Spectroscopic Methodology and Molecular Docking Studies on Changes in Binding Interaction of Felodipine with Bovine Serum Albumin Induced by Cocrystallization with β-Resorcylic Acid.

Spectroscopic Methodology and Molecular Docking Studies on Changes in Binding Interaction of Felodipine with Bovine Serum Albumin Induced by Cocrystallization with β-Resorcylic Acid. Chem Pharm Bull (Tokyo). 2020;68(10):946-953 Authors: Li C, Du P, Zhou M, Yang L, Zhang H, Wang J, Yang C Abstract In the present study, a novel cocrystal of felodipine (FEL) and β-resorcylic acid (βRA) was developed. We specially focused on the change of binding pattern with bovine serum albumin (BSA) induced by cocrystallization of FEL with βRA. The solid characterizations and density functional theory (DFT) simulation verified that FEL-βRA cocrystal formed in equimolar ratio (1 : 1 M ratio) through C=O…H-O hydrogen bond between C=O group in FEL and O-H group in βRA. The binding interactions between FEL-βRA system and BSA were studied using fluorescence spectral and molecular docking methods. Two guest molecule systems, including a physical mixture of FEL and βRA and FEL-βRA cocrystal were performed binding to BSA in molecular docking. According to the Kb and binding energy, the supramolecular form of FEL-βRA system was retained during binding to BSA. Molecular docking simulation suggested that FEL and its cocrystal inserted into the subdomain IIIA (site II') of BSA. The interactions between FEL and BSA including hydrogen bonding with ASN390 residue and intermolecular hydrophobic interactions with LEU429 and LEU452 residues. However, ...
Source: Chemical and Pharmaceutical Bulletin - Category: Drugs & Pharmacology Authors: Tags: Chem Pharm Bull (Tokyo) Source Type: research