Molecular docking, a tool to determine interaction of CuO and TiO2 nanoparticles with human serum albumin

Abstract

Background: We study the human serum albumin (HSA) protein-CuO nanoparticle interaction to identify the specific binding site of protein with CuO nanoparticles by molecular docking and compared it with HSA-TiO2 nanoparticle interaction. Methods: The protein structural data that was obtained using Autodock 4.2. Results: In case of CuO np-HSA interaction, the distances from the centre of Subdomain IIIA to Arg-472 is 2.113 Å and Lys 475, Glu 492, Ala 490, Cys 487, Ala 490 are the bound neighbouring residues with Lys 475, Glu 492 at aliphatic region. The binding energy generated was -1.64 kcal mol-1. However, for TiO2 nanoparticle, the binding region is surrounded by Arg 257, Ala 258, Ser 287, His 288, Leu 283, Ala 254, Tyr 150 (subdomain II A) as neighbouring residue. Moreover, Glu 285, Lys 286 forms aliphatic grove for TiO2-HSA, Ser-287 at the centre region form hydrogen bond with nanoparticle and Leu 283, Leu 284 forming hydrophopobic grove for TiO2 nanoparticle-HSA interaction. The binding energy generated was -2.47 kcal mol-1. Conclusions: Analysis suggests that CuO bind to suldow site II i.e subdomain III A of HSA protein where as TiO2 nanoparticle bind to suldow site I i.e subdomain IIA of HSA protein. General significance: The structural information that derives from this study for CuO and TiO2 nanoparticles may be useful in terms of both high and low-affinity binding sites when designing these nanoparticles based drugs delivery system.