Abstract

A Docking Study: Modeling of BSA-Metal Ion-polycomplexes of Poly (Methyl Vinyl Ether-CO- Maleic Anhydride)

Vildan Enisoolu Atalay, Ibrahim Baris Oluc and Mesut Karahan

Üsküdar University, Department of Bioengineering, Istanbul, TURKEY.

DOI : http://dx.doi.org/10.29055/jccs/667

ABSTRACT

The best known function of albumin is protein constructs that allow the transport of a large number of chemical compounds. Many endogenous and exogenous compounds are transported into the bloodstream after complexing with serum albumin. In order to understand the nature of the transport and distribution of these compounds within biological organisms, it is important to examine the interactions of ions and molecules with proteins. In this work, the binding constants of experimentally studied metal-BSA complexes were calculated by using computational chemistry and molecular docking methods. Bovine serum albumin (BSA, pdb code: 4OR0), polycomplexes of poly (methyl vinyl ether-CO-maleic anhydride) (PMVEMA) and eight different metal ions (Cd+2, Co+2, Cu+1, Cu+2, Fe+2, Fe+3, Ni+2 and Zn2+) were investigated by molecular docking study. The study was carried out in two stages: As the first step, the stability of the complexes was calculated by the semi-emprical PM6 method, in which Spartan16’, GaussView5.0 and Gaussian09 programs were used. In the second step, the complex formation energies of the stable ligands were performed using AutoDock Vina. BSA-Co+2-PMVEMA complex is found to be the most stable complex in all the metal complexes for docking studies.

Keywords :Molecular Docking, BSA, PM6, binding energy, metal complex.