Molecular interaction of human serum albumin with paracetamol: Spectroscopic and molecular modeling studies |
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| Authors: | Parandis Daneshgar Ali Akbar Moosavi-Movahedi Parviz Norouzi Mohammad Reza Ganjali Armin Madadkar-Sobhani Ali Akbar Saboury |
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| Institution: | 1. Center of Excellence in Electrochemistry, University of Tehran, Tehran, Iran;2. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;3. Foundation for Advancement of Science and Technology in Iran (FAST-IR), Tehran, Iran;4. Endocrinology & Metabolism Research Center, Medical Sciences/University of Tehran, Tehran, Iran |
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| Abstract: | The interaction between paracetamol and human serum albumin (HSA) under physiological conditions has been investigated by fluorescence, circular dichroism (CD) and docking. Fluorescence data revealed that the fluorescence quenching of HSA by paracetamol was the result of the formed complex of HSA–paracetamol, and the binding constant (Ka) and binding number obtained is 1.3 × 104 at 298 K and 2, respectively for the primary binding site. Circular dichorism spectra showed the induced conformational changes in HSA by the binding of paracetamol. Moreover, protein–ligand docking study indicated that paracetamols (two paracetamols bind to HSA) bind to residues located in the subdomain IIIA. |
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