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Physical Chemistry Chemical Physics


Insights into the Molecular Interaction between Two Polyoxygenated Cinnamoylcoumarin Derivatives and Human Serum Albumin


Authors: Anahita Khammari; Ali Akbar Saboury; Mohammad Hossein Karimi-Jafari; Mehdi Khoobi; Atiyeh Ghasemi; Saeed Yousefinejad; Osama K. Abou-Zied

Publication Date: -0001-11-30  Article ASAP

Ligand binding studies on human serum albumin (HSA) are crucial in pharmacological properties determination of drug candidates. Here, two representatives of coumarin–chalcone hybrids were selected and their binding mechanism was identified via thermodynamics techniques, curve resolution analysis and computational methods at molecular levels. The binding parameters were derived using spectroscopic approaches and the results point to only one pocket located near Trp214 residue in subdomain IIA of HSA. The protein tertiary structure was altered during the ligand binding and formed an intermediate structure to create stronger ligand binding interactions. The best binding mode of ligand was initially estimated by docking on an ensemble of HSA crystallographic structures and by molecular dynamics (MD) simulations. Per residue interaction energies were calculated over the MD trajectories as well. Reasonable agreement was found between experimental and theoretical results about the nature of binding that was dominated by hydrogen bonding and van der Waals contributions.  Read more