Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 45, Issue 2, Pages 129-134Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2009.04.011
Keywords
Paracetamol; Human serum albumin; Docking; Binding residues; Fluorescence spectroscopy; Circular dichroism
Funding
- research council of the University of Tehran
- Iran National Science Foundation (INSF)
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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 (K-a) and binding number obtained is 1.3 x 10(4) 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. (C) 2009 Elsevier B.V. All rights reserved.
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