Abstract
7-Geranyloxycoumarin (auraptene; AUR), as a potent phytochemical, is the naturally abundant prenyloxycoumarin found in many genera of the Rutaceae family. As the interaction with serum albumins may play a crucial role in identifying their pharmacological properties, we investigated AUR binding profile with bovine serum albumin (BSA) by experimental and computational methods. Binding constant, binding site, mode of binding, and the BSA structural change upon AUR addition, were studied. UV–vis spectroscopy results and fluorescence quenching analysis proposed that AUR can form the ground state complex with BSA. Meantime, thermodynamic parameters (negative ΔH and ΔS values) revealed that hydrogen bonds and van der Waals interactions play major role, as intermolecular forces, in the AUR–BSA complex formation. Synchronous fluorescence spectra and circular dichroism (CD) data showed that the secondary structure of BSA did not change significantly in the presence of AUR. Moreover, molecular docking results showed that AUR binds to the subdomain IIIB of BSA.
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