Add time:08/12/2019         Source:sciencedirect.com

The interaction between the transport protein bovine serum albumin (BSA) and the natural product lophirone B, was investigated by spectroscopic techniques combined with a computational method (molecular docking). From the KSV and kq values it was concluded that lophirone B quenches the fluorescence of BSA by dynamic and static mechanisms. The Ka values, of the order of 104 M−1, and the number of binding sites (n ≈ 1), indicate that the binding is moderate and there is just one main binding site in BSA for lophirone B. The negative ΔG° values are in accordance with the spontaneity of the process and the positive ΔH° and ΔS° values indicate that the binding is entropically driven; the main binding forces for the association BSA:lophirone B are probably lipophilic interactions. Circular dichroism (CD) studies show there is not a significant perturbation on the secondary structure of the albumin upon the binding process. In order to better understand the spectroscopic results, a computational method was applied: molecular docking suggests Trp-213 site, as the main binding site for the ligand. Lophirone B seems to be exposed to the aqueous media as well as accommodated inside the protein cavity, resulting in a moderate affinity for the albumin. The Arg-198, His-287, Lys-294 and Lys-439 residues are interacting via hydrogen bonding with lophirone B, whereas the interaction with Trp-213 residue occurs through a lipophilic interaction.

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