Interaction of Emodin and its Derivative Frangulin-A with Bovine Serum Albumin and Calf Thymus DNA

The interaction between emodin, frangulin-A (obtained from Ventilago leiocarpa Benth) with bovine serum albumin (BSA), and calf thymus DNA (ct-DNA) has been investigated. The fluorescence spectrum and molecular docking methods are used to investigate the interaction between emodin, frangulin-A, and BSA. The UV spectrum revealed interaction between emodin, frangulin-A, and ct-DNA. The fluorescence spectrum confirmed that the compounds of emodin–BSA and frangulin-A–BSA were formed showing fl uorescence quenching and a decrease of the maximum emission wavelength. The simulated molecular docking showed stable combinations of emodin–BSA and frangulin-A– BSA. Thus, molecular interactions mainly occur due to hydrophobic forces and hydrogen bonds. According to the UV spectrum, emodin and frangulin-A interacted with ct-DNA via electrostatic interaction.